prof. dr. R. (Rolf) Boelens
Gegenereerd op 2018-09-22 13:10:15

Biomoleculaire NMR Spectroscopie

De groep bestudeert de structuur en dynamica van eiwit en eiwit-DNA complexen betrokken bij gen regulatie, transcriptie en herstel van DNA schade. Voor dit onderzoek gebruikt ze hoge resolutie NMR spectroscopie en ontwikkelt hiervoor nieuwe methoden.

Gegenereerd op 2018-09-22 13:10:15
Curriculum vitae Download PDF


Prof. Rolf Boelens (1951) studied physical chemistry at the University of Groningen (Netherlands). He completed his Ph.D. in the Department of Biochemistry of the University of Amsterdam with a study on ligand binding and electron transfer in cytochrome c oxidase using EPR. For a postdoc he went to the NMR group of Robert Kaptein. Currently he is professor of biomolecular NMR spectroscopy at Utrecht University. From 2014-2016 he was head of the Department of Chemistry.

He studies structure and dynamics of proteins and protein complexes, with emphasis on protein-DNA complexes in transcription and DNA repair, and develops methods for biomolecular NMR and computational modeling of biomolecular interactions. His research resulted in over 340 publications (> 14000 citations, h-index 63).

He participated in a number of European projects such as the structural genomics project SPINE2-Complexes, coordinated the NDDP project for modeling protein-drug interactions using NMR data and the Joint Research Activities of the European Research Infrastructure projects EUNMR, EastNMR and BioNMR. He is co-organizer of the EMBO school on Multidimensional NMR in Structural Biology and coordinates the European Research Infrastructure for NMR, X-rays and EM for Translational Research (iNEXT).

Gegenereerd op 2018-09-22 13:10:15

Researcher ID: B-4702-2009

ORCID ID: 0000-0002-6939-8913

Google Scholar Citations



D Das, M Faridounnia, L Kovacic, R Kaptein, R Boelens and GE Folkers (2017) Single-stranded DNA Binding by the Helix-Hairpin-Helix Domain of XPF Protein Contributes to the Substrate Specificity of the ERCC1-XPF Protein Complex, J Biol Chem. 292, 2842-2853, DOI: 10.1074/jbc.M116.747857



A Vavrinska, J Zelinka, J Sebera, V Sychrovsky, R Fiala, R Boelens, V Sklenar, L Trantirek (2016) Impact of nucleic acid self-alignment in a strong magnetic field on the interpretation of indirect spin-spin interactions, J Biomol NMR 64, 53-62, and erratum in J Biomol NMR 65 (2016), 49

Zhang R, Loers G, Schachner M, Boelens R, Wienk H, Siebert S, Eckert T, Kraan S, Rojas-Macias MA, Lütteke T, Galuska SP, Scheidig A, Petridis AK, Liang S, Billeter M, Schauer R, Steinmeyer J, Schröder JM, Siebert HC (2016) Molecular Basis of the Receptor Interactions of Polysialic Acid (polySia), polySia Mimetics, and Sulfated Polysaccharides, ChemMedChem 11, 990-1002

Zeinab Anvarian, Hisashi Nojima, Tobias Madl, Eline van Kappel, Maureen Spit, Martin Viertler, Ingrid Jordens, Teck Low, Revina Scherpenzeel, Ineke Kuper, Klaus Richter, Albert J.R. Heck, Rolf Boelens, Jean-Paul Vincent, Stefan G. D. Rüdiger, Madelon M. Maurice (2016) Cancer mutations derail Wnt signalling via conformational conversion of the scaffold protein Axin, Nature Structural and Molecular Biology 23, 324-332

Ramachandra Dongre, Gert E. Folkers, Claudio O. Gualerzi, Rolf Boelens and Hans Wienk (2016) A model for the interaction of the G3 subdomain of Geobacillus stearothermophilus IF2 with the 30S ribosomal subunit, Protein Science 251722-33DOI: 10.1002/pro.2977

Sandra Constant, Hans L. J. Wienk, Augustinus E. Frissen, Peter de Peinder, Rolf Boelens, Daan S. van Es, Ruud J. H. Grisel, Bert M. Weckhuysen, Wouter J. J. Huijgen, Richard J. A. Gosselink and Pieter C. A. Bruijnincx (2016) New insights into the structure and composition of technical lignins: a comparative characterisation study, Green Chem., 18, 2651-2665, DOI: 10.1039/C5GC03043A

Luciana Coutinho de Oliveira, Diorge Paulo Souza, Gabriel Umaji Oka, Filipe da Silva Lima, Ronaldo Junio Oliveira, Denize Cristina Favaro, Hans Wienk, Rolf Boelens, Chuck Shaker Farah and Roberto Kopke Salinas (2016) VirB7 and VirB9 interactions are required for the assembly and antibacterial activity of a type IV secretion system, Structure, 24, 1707-1728



Tessa Sinnige, Markus Weingarth, Mark Daniëls, Rolf Boelens, Alexandre M.J.J. Bonvin, Klaartje Houben, Marc Baldus (2015) Conformational Plasticity of the POTRA 5 Domain in the Outer Membrane Protein Assembly Factor BamA, Structure 23, 1317-1324

Tessa Sinnige, Klaartje Houben, Iva Pritisanac, Marie Renault, Rolf Boelens, Marc Baldus (2015) Insight into the conformational stability of membrane-embedded BamA using a combined solution and solid-state NMR approach, J. Biomol. NMR 61, 321-332

Maryam Faridounnia, Hans Wienk, Lidija Kovacic, Gert E. Folkers, Nicolaas G.J. Jaspers, Robert Kaptein, Jan H.J. Hoeijmakers and Rolf Boelens, (2015) The Cerebro-oculo-facio-skeletal Syndrome Point Mutation F231L in the ERCC1 DNA Repair Protein Causes Dissociation of the ERCC1-XPF Complex, J. Biol. Chem. 290, 20541-20555

Samuel Furse, Hans Wienk, Rolf Boelens, Anton I.P.M. de Kroon, J. Antoinette Killian (2015) E. coli MG1655 modulates its phospholipid composition through the cell cycle, FEBS Lett 589, 2726–2730

Lidia Nieto, Inga M. Tharun, Mark Balk, Hans Wienk, Rolf Boelens, Christian Ottmann, Lech-Gustav Milroy, and Luc BrunsveldEstrogen Receptor Folding Modulates cSrc Kinase SH2 Interaction via a Helical Binding Mode, ACS Chem. Biol. 10, 2624–2632



Roberta Spadaccini, Carmine Ercole, Giuseppe Graziano, Rainer Wechselberger, Rolf Boelens and Delia Picone, Mechanism of 3D domain swapping in Bovine Seminal Ribonuclease, FEBS Journal 281, 842-850,DOI: 10.1111/febs.12651

G. Elif Karagöz, Afonso M.S. Duarte, Elias Akoury, Hans Ippel, Jacek Biernat, Tania Morán Luengo, Martina Radli, Tatiana Didenko, Bryce A. Nordhues, Dmitry B. Veprintsev, Chad Dickey, Eckhard Mandelkow, Markus Zweckstetter, Rolf Boelens, Tobias Madland Stefan G.D. Rüdiger, Molecular basis for specificity in chaperone action. Chaperoning of disordered Tau by Hsp90, Cell 156, 963-974

Roel Deckers, Sara M. Sprinkhuizen, Bart J. Crielaard, Hans J. Ippel, Rolf Boelens, Chris J.G. Bakker, Gert Storm, Twan Lammers and Lambertus W. BartelsDynamic absolute MR thermometry using nanocarriers, Contrast Media Mol. Imaging 9, 283–290

Matija Popovic, Hans Wienk, Maristella Coglievina, Rolf Boelens, Sandor Pongor and Alessandro Pintar, The basic helix–loop–helix region of the transcriptional repressor hairy and enhancer of split 1 is preorganized to bind DNA, Proteins 82, 537-45. doi: 10.1002/prot.24507

Marcel Scheepstra, Lidia Nieto, Anna. K. H. Hirsch, Sascha Fuchs, Seppe Leysen, Chan Vinh Lam, Leslie in het Panhuis, Stan van Boeckel, Hans Wienk, Rolf Boelens, Christian Ottmann, Lech-Gustav Milroy, Luc Brunsveld, Natural compound honokiol dual targets a dynamic NR-coactivator interface, Angew. Chemie 53, 6443-6448

Fariha Khan, Mark A. Daniëls, Gert E. Folkers, Rolf Boelens, S. M. Saqlan Naqvi and Hugo van Ingen,Structural basis of nucleic acid binding by Nicotiana tabacum glycine-rich RNA binding protein: implications for its RNA chaperone function, Nucleic Acid Res. 42, 8705-8718

Panagiotis L. Kastritis, João P. Rodrigues, Gert E. Folkers, Rolf Boelens and Alexandre M.J.J. Bonvin, Proteins feel more than they see: Fine-tuning of binding affinity by properties of the non-interacting surface, J. Mol. Biol. 426, 2632-2652

Lisa Tuppo, Roberta Spadaccini, Claudia Alessandri, Hans Wienk, Rolf Boelens, Ivana Giangrieco, Maurizio Tamburrini, Adriano Mari, Delia Picone and Maria Antonietta Ciardiello, Structure, stability and IgE binding of the peach allergen Peamaclein (Pru p 7), Pept. Sci. 102, 416-425

Jan Weiss, Hams Wienk, Rolf Boelens, Andre Lashewsky, Block Copolymer Micelles with an Intermediate Star-/Flower-Like Structure Studied by 1H NMR Relaxometry, Macromol Chem. Phys. 215, 915-919, DOI: 10.1002/macp.201300753

Fleur M. Ferguson, David M. Dias, João P. G. L. M. Rodrigues, Hans Wienk, Rolf Boelens, Alexandre M. J. J. Bonvin, Chris Abell, and Alessio Ciulli, Binding Hotspots of BAZ2B Bromodomain: Histone Interaction Revealed by Solution NMR Driven Docking, Biochemistry 53, 6706-6716



Henry G Hocking, Gerrit J Gerwig, Sebastien Dutertre, Aude Violette, Philipe Favreau, Reto Stocklin, Johannis P Kamerling, Rolf Boelens, Structure of the O-Glycosylated Conopeptide CcTx from Conus consors Venom, Chemistry 19, 870-879

Cornelia G. Spruijt, Felix Gnerlich, Arne H. Smits, Toni Pfaffeneder, Pascal W.T.C. Jansen, Christina Bauer, Martin Münzel, Mirko Wagner, Markus Müller, Fariha Khan, H. Christian Eberl, Anneloes Mensinga, Arjen Brinkman, Konstantin Lephikov, Udo Müller, Jörn Walter, Rolf Boelens, Hugo van Ingen, Heinrich Leonhardt,Thomas Carell and Michiel Vermeulen, Dynamic readers for 5-(hydroxy)methylcytosine and its oxidized derivatives, Cell (2013) 152, 1146-1159

Marrit Putker, Tobias Madl, Harmjan R. Vos, Hesther de Ruiter, Arne Smolders, Marieke Visscher, Maaike C.W. van den Berg, Mohammed Kaplan, Bart P. Braeckman, Hendrik C. Korswagen, Rolf Boelens, Michiel Vermeulen, Boudewijn M.T. Burgering and Tobias B. Dansen, Redox-dependent control of FOXO/DAF-16 by transportin-1, Molecular Cell (2013) 49, 730-742

Gerrit J Gerwig, Henry G Hocking, Reto Stocklin, Johannes P Kamerling and Rolf Boelens, Glycosylation of conotoxins, Marine Drugs 11, 632-642 (review)

Jiri Emmer, Andrea Vavrinska, Vladimir Sychrovsky, Ladislav Benda, Zdenek Kriz, Jaroslav Koca, Rolf Boelens, Vladimir Sklenar, and Lukas Trantirek, Influence of the O-phosphorylation of serine, threonine and tyrosine in proteins on the amidic 15N chemical shielding anisotropy tensors, J Biomol NMR 55, 59-70

J. H. van der Kolk, R. Boelens, S. B.A. Halkes, I. D. Wijnberg, M. G.M. de Sain-van der Velden,& J. H. Ippel, Some notes on fatal acquired multiple acyl-CoA dehydrogenase deficiency (MADD) in a two-year-old warmblood stallion and European tar spot (Rhytisma acerinum), Veterinary Quarterly  33 (2013), 51-55, DOI:10.1080/01652176.2012.758904

Leonardus M.I. Koharudin, Rolf Boelens, Rob Kaptein and Angela M. Gronenborn (2013), A NMR guided approach for CsrA – RNA crystallization, J Biomol NMR 56, 31-39, DOI: 10.1007/s10858-013-9712-3

Karine Loth, Manuel Gnida, Julija Romanuka, Robert Kaptein and Rolf Boelens (2013), Sliding and target location of DNA-binding proteins: An NMR view of the lac repressor system, J Biomol NMR 56, 41-49DOI: 10.1007/s10858-013-9723-0

C. Petrel, H. G. Hocking, M. Reynaud, G. Upert, Ph. Favreau, D. Biass, M. Paolini-Bertrand, S. Peigneur, J. Tytgat, N. Gille, O. Hartley, R. Boelens, R. Stocklin, D. Servent, Identification, structural and pharmacological characterization of ?-CnVA, the first conopeptide interacting with somatostatin sst3 receptor, Biochem. Pharmacology 85, 1663-71, DOI:

Ana C. da Silva Almeida, Henry G. Hocking, Rolf Boelens, Agnes G S H van Rossum and Ger J. Strous, βTrCP interacts with the ubiquitin-dependent endocytosis motif of the GH receptor in an unconventional manner, Biochemical Journal 453, 291-301

Wienk H, Slootweg JC, Speerstra S, Kaptein R, Boelens R, Folkers GE (2013) The Fanconi anemia associated protein FAAP24 uses two substrate specific binding surfaces for DNA recognition, Nucl Acids Res 41, 6739-49

van Nuland R, van Schaik FMA, Simonis M, van Heesch S, Cuppen E, Boelens R, Timmers HThM, van Ingen H (2013) Nucleosomal DNA binding drives the recognition of H3K36 methylated nucleosomes, Epigenetics & Chromatin 6:12, DOI:10.1186/1756-8935-6-12



S.M. Sprinkhuizen, C.J. Bakker, J.H. Ippel, R. Boelens, M.A. Viergever and L.W. Bartels, Temperature dependence of the magnetic volume susceptibility of human breast fat tissue: an NMR study, Magma 25 (2012), 33-39

Kovacic L and Boelens R, Protein-DNA interactions, in NMR of Biomolecules Towards Mechanistic Systems Biology (Bertini, I. / McGreevy, K. S. / Parigi, G, eds), Wiley-VCH, 2012

Philippe Favreau, Evelyne Benoit, Henry G. Hocking, Ludovic Carlier, Dieter D’hoedt, Enrico Leipold, René Markgraf, Sébastien Schlumberger, Marco A. Córdova, Hubert Gaertner, Marianne Paolini-Bertrand, Oliver Hartley, Jan Tytgat, Stefan H. Heinemann, Daniel Bertrand, Rolf Boelens, Reto Stöcklin, and Jordi Molgó, Pharmacological characterization of a novel ?-conopeptide, CnIIIC, indicates potent and preferential inhibition of sodium channel subtypes (NaV1.2/1.4) and reveals unusual activity on neuronal nicotinic acetylcholine receptors, British Journal of Pharmacology 166, 1654-1668

T.A.Wassenaar, M.van Dijk,  N. Loureiro Ferreira, G. van der Schot, S.J. de Vries, J. van der Zwan, R. Boelens, A.Giachetti, D. Carotenuto, A. Rosato, I.Bertini, H.R.Jonker, A.Bagaria, V.Zharavin, P.Güntert, H. Schwalbe, W.F.Vranken, M.Verlato, S.Dal Pra, M. Mazzucato, A.M.J.J.Bonvin, “WeNMR: Structural Biology on the Grid”, Journal of GRID Computing, in press

R. Spadaccini, C. Ercole, M.A. Gentile, D. Sanfelice, R. Boelens, R. Wechselberger, G. Batta, A. Bernini, N. Niccolai and D. Picone, NMR studies on structure and dynamics of the monomeric derivative of BS-RNase: new insights for 3D domain swapping", Plos One 7, e29076, DOI: 10.1371/journal.pone.0029076; Erratum in: PLoS One. 2012;7(2). doi: 10.1371/annotation/b2acf16f-53da-4a8f-a46f-573b7f6f08b7

Wojciech Augustyniak, Agnieszka A. Brzezinska, Tjaard Pijning, Hans Wienk, Rolf Boelens, Bauke W. Dijkstra and Manfred T. Reetz, Biophysical Characterization of Mutants of Bacillus subtilis Lipase Evolved for Thermostability: Factors Contributing to Increased Activity Retention, Protein Science 21, 487-497

Das, D, Folkers, GE, van Dijk, M., Jaspers, NGJ, Hoeijmakers JHJ, Kaptein, R and Boelens R, The structure of the XPF helix-hairpin-helix domain bound to single strand DNA. A model for the binding of XPF/ERCC1 at a ss/ds DNA junction, Structure 20, 667-675

Hans Wienk, Evgeny Tishchenko, Riccardo Belardinelli, Simona Tomaselli, Ramachandra Dongre, Roberto Spurio, Gert Folkers, Claudio O. Gualerzi, and Rolf Boelens, Structural Dynamics of Translation Initiation Factor IF2, J. Biol. Chem. 287, 10922-10932

S. Stötzel, M. Schurink, H. Wienk, U. Siebler, M. Burg-Roderfeld, T. Eckert, B. Kulik, R. Wechselberger, J. Sewing, J. Steinmeyer, S. Oesser, R. Boelens and H.-C. Siebert, Molecular organization of various collagen fragments as revealed by Atomic Force Microscopy and Diffusion Ordered NMR Spectroscopy, ChemPhysChem 2012, 13, 3117-25

Marijke Hospes, Johannes H. Ippel, Rolf Boelens, Klaas J. Hellingwerf and Johnny Hendriks, Binding of hydrogen-citrate to photoactive yellow protein is affected by the structural changes related to signaling state formation, J Phys Chem B 2012, 116, 13172-182

Yanyan Li, G. Elif Karagöz, Young Ho Seo, Tao Zhang, Yiqun Jiang, Yanke Yu, Steven J. Schwartz, Rolf Boelens, Kate Carroll, Stefan G. D. Rüdiger, and Duxin Sun, Sulforaphane inhibits Hsp90 pancreatic cancer through disrupting Hsp90-p50Cdc37 complex and direct interactions with amino acids of Hsp90, J. Nutr. Biochem. 23, 1617-1626

Wojciech Augustyniak, Hans Wienk, Rolf Boelens, Manfred T. Reetz, 1H, 13C and 15N resonance assignments of wild-type Bacillus subtilis Lipase A and its mutant evolved towards thermostability, Biomol NMR Assign (2012), DOI 10.1007/s12104-012-9420

Markley JL, Akutsu H, Asakura T, Baldus M, Boelens R, Bonvin A, Kaptein R, Bax A, Bezsonova I, Gryk MR, Hoch JC, Korzhnev DM, Maciejewski MW, Case D, Chazin WJ, Cross TA, Dames S, Kessler H, Lange O, Madl T, Reif B, Sattler M, Eliezer D, Fersht A, Forman-Kay J, Kay LE, Fraser J, Gross J, Kortemme T, Sali A, Fujiwara T, Gardner K, Luo X, Rizo-Rey J, Rosen M, Gil RR, Ho C, Rule G, Gronenborn AM, Ishima R, Klein-Seetharaman J, Tang P, van der Wel P, Xu Y, Grzesiek S, Hiller S, Seelig J, Laue ED, Mott H, Nietlispach D, Barsukov I, Lian LY, Middleton D, Blumenschein T, Moore G, Campbell I, Schnell J, Vakonakis IJ, Watts A, Conte MR, Mason J, Pfuhl M, Sanderson MR, Craven J, Williamson M, Dominguez C, Roberts G, Günther U, Overduin M, Werner J, Williamson P, Blindauer C, Crump M, Driscoll P, Frenkiel T, Golovanov A, Matthews S, Parkinson J, Uhrin D, Williams M, Neuhaus D, Oschkinat H, Ramos A, Shaw DE, Steinbeck C, Vendruscolo M, Vuister GW, Walters KJ, Weinstein H, Wüthrich K, Yokoyama S., In support of the BMRB., Nat Struct Mol Biol. 19 (2012), 854-60, doi: 10.1038/nsmb.2371.



G. Elif Karagöz, Afonso M. S. Duarte, Hans Ippel, Charlotte Uetrecht, Tessa Sinnige, Martijn van Rosmalen, Jens Hausmann, Albert J. R. Heck, Rolf Boelens, and Stefan G. D. Rüdiger, N-terminal domain of human Hsp90 triggers binding to the cochaperone p23, Proc Natl Acad Sci U S A 108 (2011), 580-585

Tanya Didenko, Rolf Boelens and Stefan Rüdiger, 3D DOSY-TROSY to determine the translational diffusion coefficient of large protein complexes, Protein Eng Des Sel. 24 (2011), 99-103; Erratum in: 25 (2012), 319

Maria Noutsou, Afonso M.S. Duarte, Zeinab Anvarian, Tatiana Didenko, David P. Minde, Ineke Kuper, Isabel de Ridder, Christina Oikonomou, Assaf Friedler, Rolf Boelens, Stefan G.D. Rüdiger, Madelon M Maurice Critical Scaffolding Regions of the Tumor Suppressor Axin1 are Natively Unfolded, J. Mol. Biol.  405 (2011), 773-786

Richard G. Hibbert, Anding Huang, Rolf Boelens and Titia K. Sixma, The E3 ligase Rad18 selects for monoubiquitination rather than ubiquitin chain formation by E2 enzyme Rad6, Proc Natl Acad Sci U S A 108, 5590-5595

Christian Koehler, Ludovic Carlier, Daniele Veggi, Enrico Balducci, Federica Di Marcello, Mario Ferrer-Navarro, Mariagrazia Pizza, Xavier Daura,  Marco Soriani, Rolf Boelens and Alexandre M.J.J. Bonvin, “Structural and biochemical characterization of NAR E, an iron containing ADP-ribosyltransferase from neisseria meningitidis”, J. Biol. Chem 286, 14842-14851

A. Neumoin, A. Leonchiks, P. Petit, L. Vuillard, M. Pizza, M. Soriani, R. Boelens and A.M.J.J. Bonvin. 1H, 13C and 15N assignment of the GNA1946 outer membrane lipoprotein from Neisseria meningitidis”, Biomol NMR Assign 5, 135-138

L. Carlier, C. Koehler, D. Veggi, M. Pizza, M. Soriani, R. Boelens and A.M.J.J. Bonvin, "NMR resonance assignments of NarE, a putative ADP-ribosylating toxin from Neisseria meningitides", Biomol. NMR Assign 5, 35-38

Anding Huang, Richard G. Hibbert, Rob Jong, Devashish Das, Titia K. Sixma and Rolf Boelens, Symmetry and asymmetry of the RING-RING dimer of Rad18, J Mol Biol 410, 424-435

Dirk Stratmann, Rolf Boelens, and Alexandre M.J.J. Bonvin, “Quantitative use of 1H? chemical shifts for the modelling of protein complexes “, PROTEINS: Structure, Function, and Bioinformatics 79, 2662-2670

Imre Berger, Alexandre G. Blanco, Rolf Boelens, Jean Cavarelli, Michael Coll, Gert E. Folkers, Yan Nie, Vivian Pogenberg, Patrick Schultz, Mathias Willmans, Dino Moras and Arnaud Poterszman, Structural insights into transcription complexes, J Struct Biol. 175, 135-46 (review)

Peters F, Maestre-Martinez M, Leonov A, Kovacic L, Becker S, Boelens R and Griesinger C, Cys-Ph-TAHA: a lanthanide binding tag for RDC and PCS enhanced protein NMR, J Biomol NMR. 2011, 51, 329-337


Brondijk TH, de Ruiter T, Ballering J, Wienk H, Lebbink RJ, van Ingen H, Boelens R, Farndale RW, Meyaard L, Huizinga EG. Crystal structure and collagen-binding site of immune inhibitory receptor LAIR-1: unexpected implications for collagen binding by platelet receptor GPVI. Blood 115 (2010), 1364-73

Krzeminski M, Loth K, Boelens R, Bonvin AM. SAMPLEX: automatic mapping of perturbed and unperturbed regions of proteins and complexes. BMC Bioinformatics 11 (2010), 51.

Diago-Navarro E, Hernandez-Arriaga AM, López-Villarejo J, Muñoz-Gómez AJ, Kamphuis MB, Boelens R, Lemonnier M, Díaz-Orejas R. parD toxin-antitoxin system of plasmid R1--basic contributions, biotechnological applications and relationships with closely-related toxin-antitoxin systems. FEBS Journal 277 (2010), 3097-117, Review

Huang A, de Jong RN, Folkers GE, Boelens R. NMR characterization of foldedness for the production of E3 RING domains. J Struct Biol 172 (2010), 120-127.

Nuno Loureiro-Ferreira , Tsjerk A. Wassenaar, Sjoerd J. de Vries, Marc van Dijk, Gijs van der Schot, Johan van der Zwan, Rolf Boelens, Andrea Giachetti, Dario Carotenuto, Antonio Rosato, Ivano Bertini, Torsten Herrmann, Anurag Bagaria, Victor Zharavin, Hendrik R.A. Jonker, Peter Güntert, Harald Schwalbe, Wim F. Vranken, Stefano Dal Pra, Mirco Mazzucato, Eric Frizziero, Sergio Traldi, Marco Verlato, Alexandre M.J.J. Bonvin, “e-NMR gLite grid enabled infrastructure”, IBERGRID’2010 conference proceedings (2010). IBERGRID, 4th Iberian Grid Infrastructure Conference Proceedings. Netbiblo, A Coruña, Spain.



Mickaël Krzeminski, Gloria Fuentes, Rolf Boelens and Alexandre M.J.J. Bonvin, “MINOES: a new approach to select a representative ensemble of structures in NMR studies of (partially) unfolded states. Application to ?25-PYP, Proteins 74 (2009), 895-904

Anding Huang, Rob Jong, Hans Wienk, G. Sebastiaan Winkler, H.Th.Marc Timmers and Rolf Boelens,  ”E2-c-Cbl recognition is necessary but not sufficient for ubiquitination activity”, J Mol Biol 385 (2009), 507-519

Romanuka J, den Bulke HV, Kaptein R, Boelens R, Folkers GE, “Novel strategies to overcome expression problems encountered with toxic proteins: application to the production of Lac repressor proteins for NMR studies”, Protein Expr Purif 67 (2009), 104-112

Romanuka J, Folkers GE, Biris N, Tischenko E, Wienk H, Bonvin AM, Kaptein R, Boelens R., “Specificity and Affinity of Lac Repressor for the Auxiliary Operators O2 and O3 Are Explained by the Structures of Their Protein-DNA Complexes”, J Mol Biol 390 (2009), 478-489

Marco Sette, Roberto Spurio, Edoardo Trotta, Anna Brandi, Cynthia L. Pon, Gaetano Barbato, Rolf Boelens and Claudio O. Gualerzi, “DNA-binding specificity of the C-terminal domain of nucleoid-associated protein H-NS”, J Biol Chem 284 (2009), 30453-30462.

Elizabeth Diago-Navarro, Monique Kamphuis, Rolf Boelens, Arjan Barendregt, Albert Heck, Robert van den Heuvel, Ramón Díaz-Orejas, “A mutagenic analysis of the RNase mechanism of the bacterial Kid toxin by mass spectrometry”, FEBS Journal 273 (2009), 4973–4986

Sjoerd J.L. van Wijk, Sjoerd J. de Vries, Patrick Kemmeren, Anding Huang, Rolf Boelens, Alexandre M. J. J. Bonvin and H. Th. Marc Timmers, “A comprehensive framework of E2-RING E3 interactions of the human ubiquitin-proteasome system”, Molecular Systems Biology 5 (2009), 295-311


Véronique Blanchard, Martin Frank,  Bas Leeflang, Rolf Boelens, Johannis Kamerling, “The structural basis of the difference in sensitivity for PNGase F in the de-N-glycosylation of the native bovine pancreatic ribonucleases B and BS”, Biochemistry 11 (2008), 3435-3446.

Devashish Das, Konstantinos Tripsianes, Nicolaas G.J. Jaspers, Jan H.J. Hoeijmakers, Robert Kaptein, Rolf Boelens and Gert E. Folkers, “The (HhH)2 domain of the human DNA repair protein XPF forms stable homodimers”, Proteins 70 (2008), 1551–1563.

Shannon M. Harper, Hans Wienk, Rainer W. Wechselberger, Johannes L. Bos, Rolf Boelens, Holger Rehmann, “Structural dynamics in the activation of EPAC”, J.Biol.Chem 283 (2008), 6501-6508.

V.Blanchard, R.A.Gadkari, A.V.George, S.Roy, G.J.Gerwig, B.R.Leeflang, R.R.Dighe, R.Boelens, J.P.Kamerling, “High-level expression of biologically active glycoprotein hormones in Pichia pastoris strains-selection of strain GS115, and not X-33, for the production of biologically active N-glycosylated 15N-labeled phCG”, Glycoconj J. 3 (2008), 245-257. 

L. Codutti, H. van Ingen, C. Vascotto, F. Fogolari, A. Corazza, G. Tell, F. Quadrifoglio, P. Viglino, R. Boelens and G. Esposito, The solution structure of DNA-free Pax-8 paired box domain accounts for redox regulation of transcriptional activity in the pax protein family, J Biol Chem 283 (2008), 33321-33328

Hugo van Ingen, Frederik M.A. van Schaik, Hans Wienk, Joost Ballering, Holger Rehmann, Annemarie C. Dechesne, John A.W. Kruijzer, Rob M.J. Liskamp, H.Th. Marc Timmers and Rolf Boelens, Structural Insight into the Recognition of the H3K4me3 mark by the TFIID subunit TAF3, Structure 16 (2008), 1245-1256


A.D. van Dijk, S. Ciofi-Baffoni, L. Banci, I. Bertini, R. Boelens and A.M.J.J. Bonvin, “Modeling protein-protein complexes involved in the cytochrome C oxidase copper-delivery pathway”, J Proteome Res. 6 (2007), 1530-1539

M.C. Monti, A.M. Hernandez-Arriaga, M.B. Kamphuis, J. Lopez-Villarejo, A.J.R. Heck, R. Boelens, R. Diaz-Orejas and R.H. van den Heuvel, “Interactions of Kid-Kis toxin-antitoxin complexes with the parD operator-promoter region of plasmid R1 are piloted by the Kis antitoxin and tuned by the stoichiometry of Kid-Kis oligomers, Nucleic Acids Res. 35 (2007), 1737-1749

M.B. Kamphuis, M.C. Monti, R.H. an den Heuvel, J. Lopez-Villarejo, R. Diaz-Orejas and R. Boelens, “Structure and function of bacterial kid-kis and related toxin-antitoxin systems”, Protein Pept Lett. 14 (2007), 113-124, Review

M.B. Kamphuis, M.C. Monti, R.H. van den Heuvel, S. Santos-Sierra, G.E. Folkers, M. Lemonnier, R. Diaz-Orejas, A.J.R Heck AJ and R. Boelens, “Interactions between the toxin kid of the bacterial parD system and the antitoxins Kis and MazE”, Proteins 67 (2007), 219-231

M.Gauden, J.S.Grinstead, W.Laan, I.H.Stokkum, M.Avila-Perez, K.C.Toh, R.Boelens, R.Kaptein, R.V.Grondelle, K.J.Hellingwerf, J.T.Kennis, “On the Role of Aromatic Side Chains in the Photoactivation of BLUF Domains”, Biochemistry 46 (2007), 7405-7415. 

K.Tripsianes, G.E. Folkers, C.Zheng, D.Das, J.S. Grinstead, R.Kaptein and R.Boelens, “Analysis of the XPA and ssDNA-binding surfaces on the central domain of human ERCC1 reveals evidence for subfunctionalization”, Nucleic Acids Research 17 (2007), 5789-5798



J.S. Grinstead, M. Avila-Perez, K.J. Hellingwerf, R. Boelens and  R. Kaptein, “Light-induced flipping of a conserved glutamine sidechain and its orientation in the AppA BLUF domain”, J Am Chem Soc. 128 (2006), 15066-15067

P. Milon, E. Tischenko, J. Tomsic,  E. Caserta , G.E.  Folkers, A., La Teana , M.V.  Rodnina , C.L. Pon, R. Boelens and C.O.  Gualerzi, “The nucleotide-binding site of bacterial translation initiation factor 2 (IF2) as a metabolic sensor”, Proc Natl Acad Sci U S A. 103 (2006), 13962-13967

S. Tomaselli, O. Crescenzi, D. Sanfelice, E. AB, R.W. Wechselberger, S. Angeli, A. Scaloni, R. Boelens, T. Tancredi, P. Pelosi and D. Picone, “Solution structure of a chemosensory protein from the desert locust Schistocerca gregaria”, Biochemistry 45 (2006), 10606-10613

N. Sibille, A. Favier, A.I. Azuaga, G. Ganshaw, R. Bott, A.M.J.J. Bonvin, R. Boelens and  N.A.J. van Nuland, “Comparative NMR study on the impact of point mutations on protein stability of Pseudomonas mendocina lipase”, Protein Sci. 15 (2006), 1915-1927

M. van Dijk, A.D. van Dijk, V. Hsu, R. Boelens and A.M.J.J Bonvin, “Information-driven protein-DNA docking using HADDOCK: it is a matter of flexibility”, Nucleic Acids Res. 34 (2006), 3317-3325

E. AB, D.J. Pugh, R. Kaptein, R. Boelens and A.M.J.J. Bonvin, “Direct use of unassigned resonances in NMR structure calculations with proxy residues”, J Am Chem Soc. 128 (2006), 7566-7571

R.K. Salinas, T. Diercks, R. Kaptein and R.  Boelens, “Cooperative alpha-helix unfolding in a protein-DNA complex from hydrogen-deuterium exchange”, Protein Sci. 15 (2006), 1752-1759

A.D. van Dijk, R. Kaptein, R. Boelens and A.M.J.J. Bonvin, “Combining NMR relaxation with chemical shift perturbation data to drive protein-protein docking”, J Biomol NMR. 34 (2006), 237-244

H.R. Jonker, R.W. Wechselberger, R. Boelens, R. Kaptein R, and G.E. Folkers, “The intrinsically unstructured domain of PC4 modulates the activity of the structured core through inter- and intramolecular interactions”, Biochemistry. 45 (2006), 5067-5081

M.B. Kamphuis, A.M.J.J. Bonvin, M.C. Monti, M. Lemonnier, A. Munoz-Gomez, R.H. van den Heuvel, R. Diaz-Orejas and R. Boelens, “Model for RNA binding and the catalytic site of the RNase Kid of the bacterial parD toxin-antitoxin system”, J Mol Biol. 357 (2006), 115-126



A.D.J. van Dijk, R. Boelens and A.M.J.J. Bonvin, “Data-driven docking for the study of biomolecular complexes”, FEBS Journal 272 (2005), 293-312. Review

H.R. Jonker R.W. Wechselberger, R. Boelens, G.E. Folkers and R. Kaptein. “Structural properties of the promiscuous VP16 activation domain.”, Biochemistry (2005) 44, 827-39.

C. Bernard, K. Houben, N. M. Derix, D. Marks, M. A. van der Horst, K. J. Hellingwerf, R. Boelens, R. Kaptein and N.A.J. van Nuland, “The solution structure of a transient photoreceptor intermediate: ?25-Photoactive Yellow Protein”, Structure 13 (2005), 953-962.

R. Kopke Salinas, G.E. Folkers, A.M.J.J. Bonvin, D. Das, R. Boelens and R. Kaptein, “Altered specificity in DNA binding by the lac repressor: A mutant lac headpiece that mimics the gal repressor”, ChemBioChem 6 (2005), 1628-1637.

E. Kellenberger, C. Dominguez, S. Fribourg, E. Wasielewski, D. Moras, A. Poterszman, R. Boelens and B. Kieffer, “Solution structure of the C-terminal domain of TFIIH P44 subunit reveals a novel type of C4C4 ring domain involved in protein-protein interactions”, J.Biol.Chem 280 (2005),  20785-20792.

K. Houben, E. Wasielewski, C. Dominguez, E. Kellenberger,  R.A.Atkinson, H.Th.M. Timmers, B. Kieffer and R Boelens, “Dynamics and metal exchange properties of C4C4 RING domains from CNOT4 and the p44 subunit of TFIIH”, J Mol Biol 349 (2005),  621-637

K. Tripsianes, G.E. Folkers ER. AB, D. Das,  H. Odijk, N.G.J. Jaspers, J.H.J. Hoeijmakers, R. Kaptein, and R. Boelens,”The structure of the human ERCC1/XPF interaction domains reveals a complementary role for the two proteins in nucleotide excision repair” Structure 12 (2005), 1849-1858

G. Fuentes, A.J. Nederveen, R. Kaptein,  R. Boelens, and A.M.J.J. Bonvin, “Describing partially unfolded states of proteins from sparse NMR data”, J Biomol NMR 33 (2005), 175-86

J.S. Grinstead, S.T. Hsu, W. Laan, A.M.J.J Bonvin, K.J. Hellingwerf, R. Boelens and  R. Kaptein, “The solution structure of the AppA BLUF domain: insight into the mechanism of light-induced signaling”, Chembiochem 7 (2006), 187-193

A.M.J.J Bonvin, R. Boelens and R. Kaptein, “NMR analysis of protein interactions”, Curr Opin Chem Biol. 9 (2005),  501-508, Review.

H. Wienk, S. Tomaselli, C. Bernard,  R. Spurio, D. Picone , C.O.  Gualerzi and R.  Boelens, “Solution structure of the C1-subdomain of Bacillus stearothermophilus translation initiation factor IF2”, Protein Sci. 14 (2005), 2461-2468



C.Dominguez, A.M.J.J. Bonvin, G. S.Winkler, F.M.A. van Schaik, H. Th. M.Timmers and R.Boelens, "Structural model of the UbcH5B/CNOT4 complex revealed by combining NMR, mutagenesis and docking approaches." Structure 12 (2004), 633-644.

G.S. Winkler, T.K.Albert, C.Dominguez, Y.I.A.Legtenberg, R.Boelens and H.Th.M Timmers, “An altered-Specifity Ubiquitin-Conjugating Enzyme/Ubiquiting-Protein Ligase Pair”, J. Mol. Biol. 337 (2004), 157-165.

C.Dominguez, G.E. Folkers, R.Boelens, “Ring domain proteins”, Handbook of Metalloproteins. 3 (2004), 338-350.

M.A. Durney,  R.W. Wechselberger, C.G. Kalodimos, R. Kaptein, C.E. Vorgias, R. Boelens,
“An alternate conformation of the hyperthermostable HU protein from Thermotoga maritima has unexpectedly high flexibility”, FEBS Letters 563/1-3 (2004), 49-54.

K. Houben and R. Boelens,  “Side chain dynamics monitored by 13C-13C cross-relaxation”, J.Biomol.NMR 29 (2004), 151-166.

C.G.Kalodimos, N. Biris, A.M.J.J.Bonvin, M.M.Levandoski, M.Guennuegues, R. Boelens and R. Kaptein,  “Structure and Flexibility Adaptation in Nonspecific and Specific Protein-DNA Complexes”, Science 305 (2004), 386-389.

C.G.Kalodimos, R. Boelens and R. Kaptein,  “Toward an Integrated Model of Protein-DNA Recognition as Inferred from NMR Studies on the Lac Repressor System”, Chem.Rev. 104 (2004), 3567-3586.

K.Houben, C.Dominguez, F.M.A. van Schaik, H.Th.M. Timmers, A.M.J.J. Bonvin and R. Boelens, "Solution structure of the ubiquitin-conjugating enzyme UbcH5B", J. Mol. Biol. 334 (2004), 513-526



M.C.Feiters, A.P.A.M.Eijkelenboom, H.-F. Nolting, B.Krebs, F.M.I. van den Ent,  R.H.A.Plasterk, R.Kaptein and R.Boelens,  “X-ray Absorption Spectroscopic Studies of Zinc in the N-Terminal Domain of HIV-2 Integrase and Model Compound”, J.Synchrotron Radiat. 10 (2003), 86-95.

C. Dominguez, R. Boelens and A.M.J. J. Bonvin, “HADDOCK: A protein-protein docking approach based on biochemical or biophysical  information”, J.Amer.Chem.Soc. 125 (2003), 1731-1737.

L.M.I.Koharudin, A.M.J.J.Bonvin, R.Kaptein and R.Boelens, “Use of very longdistance NOEs in a fully deuterated protein: an approach for rapid protein fold determination”, J.Magn.Reson. 163 (2003), 228-235.

N.M. Derix, R.W.Wechselberger, M.A. van der Horst, K.J.Hellingwerf, R. Boelens, R. Kaptein and N.A.J. van Nuland, “Lack of negative charge in the E46Q mutant of Photoactive Yellow Protein prevents partial unfolding of the blue shifted intermediate”, Biochemistry 42 (2003), 14501-14506.

V.V. Klochkov, B.V. Hairutdinov, A.V. Klochkov, R.A. Shaihutdinov, E.V. Tischenko,  R. Boelens and R. Kaptein,  “NMR spectroscopy in structural studies of organic and bioorganic lyotropic liquid crystalline systems”, Structure and dynamics of molecular systems 10 (2003), 5-13.



Th. K. Albert, H. Hanzawa, Y. I.A. Legtenberg, M.J. de Ruwe, F.A.J. van den Heuvel, M.A. Collart, R. Boelens and H.Th. M. Timmers, “Identification of a ubiquitin-protein ligase subunit within the CCR4-NOT transcription repressor complex”,  EMBO J. 21, 355-364.

R. Boelens and C.O. Gualerzi, “Structure and Function of Bacterial Initiation Factors”, 
Current Protein and Peptide Science. 3  (2002), 107-119s

C.G.Kalodimos, R.Boelens and R.Kaptein, “A Residue-Specific View of the Association and Dissociation Pathway in Protein-DNA Recognition”, Nature Struct. Biol. 9 (2002),193-197.  

C.G Kalodimos, A.M.J.J. Bonvin, R.Kopke Salinas, R. Wechselberger, R. Boelens and R. Kaptein, “Plasticity in Protein-DNA Recognition: lac Repressor Interacts with its Natural Operator O1 through Alternative Conformations of its DNA-Binding Domain” ,  EMBO J. 21 (2002), 2866-2876

D. Hargreaves, R. Giraldo, S. Santos-Sierra, R. Boelens, D.W. Rice, R. Díaz Orejas and J.B. Raffer, “Crystallization and preliminary X-ray crystallographic studies on the parD-encoded protein Kid from Escheridchia coli plasmid R1”, Acta Crystallogr. D58 (2002), 355-358.

D. Hargreaves, S. Santos-Sierra, R. Giraldo, R. Sabariegos-Jareño, G. de la Cueva-Méndez, R. Boelens, R. Díaz-Orejas and J.B. Rafferty, “Structural and Functional Analysis of the Kid Toxin Protein from E. coli Plasmid R1”, Structure 10 (2002), 1425-1433.

S. Singh, G.E. Folkers, A.M.J.J. Bonvin, R. Boelens, R. Wechselberger, A. Niztayev and R. Kaptein,
“Solution Structure and DNA Binding Properties of the C-Terminal Domain of UvrC from E-coli”,  EMBO J. 21 (2002), 6257-6266.



G.E.Folkers, H.Hanzawa and R.Boelens, “Zinc Finger Proteins”in “Handbook on Metalloproteins”, I.Bertini, A.Sigel and H.Sigel, eds., M.Dekker, New York, Basel (2001), 961-1000.

H. Hanzawa, M.J. de Ruwe, Th.K. Albert, P.C. van der Vliet, H.Th.M. Timmers and R.Boelens,
“The structure of the C4C4 RING finger of human NOT4 reveals features distinct from C3HC4 RING fingers”,  J.Biol.Chem. 276 (2001), 10185-10190. 

C.G. Kalodimos, G.E. Folkers, R. Boelens and R. Kaptein, “Strong DNA binding by covalently-linked dimeric Lac headpiece: Evidence for the crucial role of the hinge helices”, PNAS 98  (2001), 6039-6044.

A.M.J.J. Bonvin, K. Houben, M. Guenneugues, R. Kaptein and R. Boelens, “Rapid protein fold determination using secondary chemical shifts and cross-hydrogen bond 15N-13C’ scalar couplings (3hbJNC’)”, J.Biomol.NMR 21 (2001), 221-233.



M.A. Nooren, G.E. Folkers, R. Kaptein, R.T. Sauer and R. Boelens, “Structure and Dynamics of the Tetrameric Mnt Repressor and a Model for its DNA Complex”,  In: Proceedings of the Eleventh Conversation in Biomolecular Stereodynamics.Vol.1.  R.H.Sarma and M.H.Sarma (eds.). Adine Press, Schenectady. 2000, pp.113-122.

M.A.A. van Tilborg, J.A. Lefstin, M. Kruiskamp, J.-M. Teuben, R. Boelens, K.R. Yamamoto, and R. Kaptein, “Mutations in the Glucocorticoic Receptor DNA-binding Domain Mimic an Allosteric Effect of DNA”, J.Mol.Biol.301 (2000) 947-958.

P.J.A. van Tilborg, M. Czisch, F.A.A. Mulder, G.E. Folkers, A.M.J.J. Bonvin, M. Nair, R. Boelens  and R. Kaptein, “Changes in Dynamical Behavior of the Retinoid X Receptor DNA-Binding Domain upon Binding to a 14 Base-Pair DNA Half Site”, Biochemistry 39 (2000) 8747-8757.

Melacini, A.M.J.J. Bonvin, M. Goodman, R. Boelens and R. Kaptein, “Hydration Dynamics of the Collagen Triple Helix by NMR”, J.Mol.Biol. 300 (2000) 1041-1048.      

A.P.A.M.Eijkelenboom, F.M.I.van den Ent, R.H.A.Plasterk, R.Kaptein and R.Boelens, “Refined solution structure of the N-terminal HHCC domain of HIV-2 integrase: flexibility at the dimer interface”, J.Biom.NMR 18 (2000) 119-128

S.C.Meunier, R.Spurio, M.Czisch, R.Wechselberger, M.Guenneugues, C.O.Gualerzi and R.Boelens,
“Structure of the fMet-tRNAfMet-binding domain of B.stearothermophilus initiation factor IF2”, EMBO J. 19 (2000) 1918-1926.

P.J.A.Erbel, Y.Karimi-Nejad, J.A.van Kuik, R.Boelens, J.P.Kamerling and J.F.G.Vliegenthart,
“Effects of the N-linked Glycans on the 3D Structure of the Free -Subunit of Human Chorionic Gonadotropin”,  Biochemistry 39 (2000) 6012-6021.

C.J. Craven, N.M. Derix, J. Hendriks, R. Boelens, K.J. Hellingwerf and R. Kaptein,
“Probing the nature of the blue-shifted intermediate of Photoactive Yellow Protein in solution by NMR: Hydrogen/Deuterium exchange data and pH studies”,  Biochemistry 39 (2000) 14392-14399

M. Guenneugues, E. Caserta, L. Brandi, R. Spurio, S. Meunier, C.L. Pon, R. Boelens and C.O.Gualerzi, “Mapping the fMet-tRNAfMet binding site of initiation factor IF2”, EMBO J. 19 (2000) 5233-5240.


G. Melacini, R. Kaptein and R. Boelens, "Editing of Chemical Exchange-Relayed NOEs in NMR Experiments for the Observation of Protein-Water Interactions", J. Magn. Res. 136 (1999), 214-218.

Y. Karimi-Nejad, F. Löhr, D. Schipper, H. Rüterjans and R. Boelens, "Gradient-purged Isotope Filter Experiments for the Detection of Bound Water in Proteins", Chem. Phys. Lett. 300 (1999) 706-712.

G. Rubinstenn, G.W. Vuister, N. Zwanenburg, K.J. Hellingwerf, R. Boelens and R. Kaptein, "NMR Experiments to study Photo-intermediates: Application to the Photoactive Yellow Protein", J. Magn. Reson 137 (1999) 443-447.

G. Melacini, R. Boelens and R. Kaptein "Band-Selective Editing of Exchange-Relay in Protein-Water NOE Experiments", J. Biomol. NMR 13 (1999), 67-71.

S. Werten, R. Wechselberger, R. Boelens, P.C. van der Vliet and R. Kaptein, "Identification of the ssDNA-Binding Surface of the Transcriptional Coactivator PC4 by NMR", J. Biol. Chem. 274 (1999) 3693-3699.

F.A.A. Mulder, P.J.A. van Tilborg, R. Kaptein, and R. Boelens, "Microsecond time scale dynamics in the RXR DNA-binding domain from a combination of spin-echo and off-resonance rotating frame relaxation measurements", J. Biomol. NMR 13 (1999) 275-288.

P.J.A. van Tilborg, F.A.A. Mulder, M.M.E. de Backer, M. Nair,  E.C. van Heerde, G. Folkers, P.T. van der Saag, Y. Karimi-Nejad, R. Boelens and R. Kaptein, "Millisecond to microsecond dynamics of the retinoid X and retinoid acid receptor DNA-binding domains and dimeric complex formation", Biochemistry 38 (1999) 1951-1956.

F.A.A. Mulder, D. Schipper, R. Bott and R. Boelens, "Altered flexibility in the substrate-binding site of related native and engineered high-alkaline Bacillus subtilisins", J. Mol. Biol. 292 (1999) 111-123.

A.P.A.M. Eijkelenboom, R. Sprangers, K. Hård, R.A. Puras Lutzke, R.H.A. Plasterk, R. Boelens  and R. Kaptein, “Refined solution structure of the C-terminal DNA-binding domain of Human Immunovirus-1 integrase”, Proteins: Structure, Function, and Genetics  36 (1999): 556-564.

M. Sette, R. Spurio, P van Tilborg, C.O. Gualerzi and R. Boelens, "Identification of the ribosome binding sites of translation initiation factor IF3 by multidimensional heteronuclear NMR spectroscopy", RNA 5 (1999), 82-92.

Y. Karimi-Nejad, F.A.A. Mulder, J.R. Martin, A.T. Brünger, D. Schipper and R. Boelens,
"NMR studies of the 269 Residue Serine Protease BP92 from Bacillus Alcalophilus", In: NMR in Supramolecular Chemistry. M Pons (ed.), Kluwer Academic Publishers. 1999, pp. 227-246.

R. Bott and R. Boelens, “The role of high-resolution structural studies in the development of commercial enzymes”, Current Opinion in Biotechnology 10 (1999) 391-397.

I.M.A. Nooren, A.W.M. Rietveld, G. Melacini, R.T. Sauer, Robert Kaptein and R. Boelens, "The solution structure and dynamics of an Arc repressor mutant reveal premelting conformational changes  related to DNA binding", Biochemistry 38  (1999) 6035-6042.

I.M.A. Nooren, R. Kaptein, R.T. Sauer and R. Boelens, “The tetramerization domain of the Mnt repressor consists of two right-handed coiled coils”, Nature Struct. Biol. 6 (1999) 755-759.

I.M.A. Nooren, A.V.E. George, Robert Kaptein, R.T. Sauer and R. Boelens,"NMR structure determination of the tetramerization domain of the Mnt: an asymmetric ?-helical assembly in slow exchange", J. Biomol. NMR 15 (1999) 39-53.

C.A.E.M. Spronk, A.M.J.J. Bonvin, P.K. Radha, G. Melacini, R. Boelens and R. Kaptein, “The  solution structure of lac repressor headpiece 62 complexed to a symmetrical lac operator sequence determined by NMR and restrained molecular dynamics”, Structure 7 (1999) 1483-1492

C.A.E.M. Spronk, A.-M. G.W. Noordman, G.W. Folders, R. Wechselberger, N. van den Brink, R. Boelens  and R. Kaptein, “Hinge-helix formation and DNA-bending in various lac repressor-operator complexes”, EMBO J. 18 (1999) 6472-6480. 

G.Melacini, R.Boelens and R. Kaptein, “Water-Macromolecule Interactions by NMR: A Quadrature-Free Constant-Time Approach”, J Biomol NMR 15, (1999) 189-201

P.J.A. Erbel, Y. Karimi-Nejad, T. de Beer, R. Boelens, J.P. Kamerling  and  J.F.G. Vliegenthart, “Solution  structure of  the  -subunit of human chorionic gonadotrpoin”, Eur.  J. Biochem. 260 (1999)  490-498.



H. Vis, C.E. Vorgias, K.S. Wilson, R. Kaptein and R. Boelens, "Mobility of NH bonds in DNA-Binding Protein HU of Bacillus stearothermophilus from Reduced Spectral Density Mapping Analysis at Multiple NMR Fields", J. Biomol. NMR 11 (1998), 265-277.

Y. Karimi-Nejad, G.L. Wareen, D. Schipper, A.T. Brünger and R. Boelens, "NMR structure calculation methods for large proteins. Application of torsion angle dynamics and distance geometry / simulated annealingto the 269-residue protein serine protease PB92", Mol. Phys. 95 (1998), 1099-1112.

F.A.A. Mulder, R.A. de Graaf, R. Kaptein and R. Boelens, "An off-resonance rotating frame relaxation experiment for the investigation of macromolecular dynamics using adiabatic rotations", J. Magn. Res. 131 (1998) 351-357.

G. Rubinstenn, G.W. Vuister, F.A.A. Mulder, P.E. Düx, R. Boelens, K.J. Hellingwerf and R. Kaptein,
"Structural and dynamic changes of photoactive yellow protein during its photocycle in solution",
Nature Struct. Biol. 5 (1998), 568-570.

M. Czisch and R. Boelens, "Sensitivity Enhancement in the TROSY Experiment", J. Magn. Res. 134 (1998) 158-160.

P. Düx, G. Rubinstenn, G.W. Vuister, R. Boelens, F.A.A. Mulder, K. Hård, W.D. Hoff, A.R. Kroon, W. Crielaard, K.J. Hellingwerf and R. Kaptein, "Solution Structure and Backbone Dynamics of the Photoactive Yellow Protein", Biochemistry 37 (1998) 12689-12699.

C.W.E.M. Thijssen-van Zuylen, T. de Beer, B.R. Leeflang, R. Boelens, R. Kaptein, J.P. Kamerling and J.F.G. Vliegenthart, "Mobilities of the Inner Three Core Residues and the Man (?1?6) Branch of the Glycan at Asn78 of the ?-Subunit of Human Chroionic Gonadrotropin Are Restricted by the Protein",
Biochemistry 37 (1998): 1933-1940.



M. Slijper, R. Boelens, A.L. Davis, R.N.H. Konings, G.A. van der Marel, J.H. van Boom and R. Kaptein,
"Backbone and sidechain dynamics of lac repressor headpiece (1-56) and its complex with DNA", Biochemistry 36, (1997) 249-254.

M. Cox, R. Boelens, P.C. van der Vliet and R. Kaptein, "Structure of the POU-domain",
In: Nucleic Acids and Molecular Biology.Vol. 11 Mechanisms of Transcription  Eds.:  F. Eckstein and D.M.J. Lilley, Springer Verlag, New York, 1997, pp. 137-150. 

R. Boelens, H. Vis, C.E. Vorgias, K.S. Wilson and R. Kaptein, "Structure and dynamics of the DNA Binding Protein HU from Bacillus stearothermophilus by NMR spectroscopy", Biopolymers 40/5 (1997) 553-339.

M. Sette, P. van Tilborg, R. Spurio, R. Kaptein, M. Paci, C.O. Gualerzi and R. Boelens, "The structure of the translational initiation factor IF1 from E. coli contains an oligomer-binding motif", EMBO J. 16 (1997) 1436-1443.

R. Kaptein, A.M.J.J. Bonvin and R. Boelens, Biomolecular Stucture and Dynamics: Recent Experimental and Theoretical Advances", In: Biomolecular Structure and Dynamics, G. Vergoten and T. Theophanides (Eds.). Kluwer Academic Publishers, 1997, pp. 189-209.

J.R. Martin, F.A.A. Mulder, Y. Karimi-Nejad, J. van der Zwan, M. Mariani, D. Schipper and R. Boelens,
"The Solution Structure of Serine Protease PB92 from Bacillus alcalophilus", Structure 5 (1997) 521-532.

M. Tessari, H. Vis, R. Boelens, R. Kaptein, and G.W. Vuister, "Quantitative Measurement of Relaxation Interference Effects between 1HN CSA and 1H-15N Dipolar Interaction: Correlation with Secondary Structure", J. Am. Chem. Soc. 119 (1997) 8985-8990.

B. Whitehead, M. Tessari, P. Düx, R. Boelens, R. Kaptein and G.W. Vuister, "An 19N-filtered 2D 1H-TOCSY experiment for assignment of aromatic ring resonances and selective identification of tyrosine ring resonances in proteins: description and application to Photoactive Yellow Protein", J. Biom. NMR 9 (1997) 313-316.

M. Tessari, F.A.A. Mulder, R. Boelens and G.W. Vuister, "Determination of Amide Proton CSA in 15N-Labeled Proteins Using 1H CSA/15N-1H Dipolar and 15N CSA/15N-1H Dipolar Cross-Correlation Rates", J. Magn. Res. 127 (1997) 128-133.

A.P.A.M. Eijkelenboom, F.M.I. van den Ent, A.Vos, J.F. Doreleijers, K. Härd, T.D. Tullius, R.H.A. Plasterk, R. Kaptein and R. Boelens, The solution structure of the N-terminal domain of HIV-2 integrase: a novel zinc-binding fold. Current Biology 7 (1997), 739-746

P. Düx, B. Whitehead, R. Boelens, R. Kaptein and G.W. Vuister, "Measurement of 15N-1H coupling constants in uniformly 15N labeled proteins. Application to the Photoactive Yellow Protein", J. Biomol. NMR 10 (1997) 301-306.



A.M.J.J. Bonvin, R. Boelens and R. Kaptein,  "Protein Structures: Relaxation Matrix Refinement", In: Encyclopedia of Nuclear Magnetic Resonance,  Vol. 6, Eds. D.M. Grant and R.K. Harris, John Wiley & Sons, Ltd., Chiserter, 1996,  pp. 3801-3811.

R. Boelens and R. Kaptein, "Homonuclear 3D NMR of biomolecules", In: Encyclopedia of Nuclear Magnetic Resonance,  Vol. 4, Eds. D.M. Grant and R.K. Harris, John Wiley & Sons, Ltd., Chiserter, 1996,  pp. 2395-2409.

R. Kaptein, M. Slijper, J.A.C. Rullmann and R. Boelens, "A bright look at Protein-DNA Complexes", Chemisch Magazine 3 (1996) 12.

E.C. van Geerestein-Ujah, M. Mariani, H. Vis, R. Boelens and R. Kaptein, "Use of Graph Theory for Secondary Structure Recognition and Sequential Assignment in Heteronuclear (13C, 15N) NMR Spectra: Application to HU Protein from Bacillus staerothermophilus", Biopolymers 39 (1996) 691-707.

R. Kaptein, M. Slijper, V.P. Chuprina, J.A.C. Rullmann, R.M.A. Knegtel and R. Boelens,
"Protein-DNA interaction from NMR and Monte Carlo Docking", In: NMR as a Structural Tool for Macromolecules Current and Future Directions, Nageswara Rao, B.D. and Kemple, M.D. Eds., Plenum Press, New York, 1996, pp. 175-187.

T. de Beer, C.W.E.M. van Zuylen, B.R. Leeflang, K. Hård, R. Boelens, R. Kaptein, J.P. Kamerling and J.F.G. Vliegenthart, "NMR Studies of the Free ?-Subunit of Human Chorionic Gonadotropin; Structural Influences of N-Glycosylation and the ?-Subunit of the Conformation of the ?-Subunit", Eur. J. Bioch. 241 (1996) 229-242.

M. Slijper, R. Kaptein and R. Boelens, "Simultaneous 13C and 15N Isotope Editing of Biomolecular Complexes. Application to a Mutant lac Repressor Headpiece DNA Complex", J. Magn. Res. B 111 (1996), 199-203.

J.F. Doreleijers, J.P.M. Langedijk, K. Hård, R. Boelens, J.A.C. Rullmann, W.M. Schaaper, J.T. van Oirschot and R. Kaptein, "Solution Structure of the Immunodominant Region of Protein G of Bovine Respiratory Syncytial Virus", Biochemistry 35 (1996) 14684-14688.

M. Slijper, A.M.J.J. Bonvin, R. Boelens and R. Kaptein, "Refined Structure of Lac Repressor Headpiece (1-56) Determined by Relaxation Matrix Calculations from 2D and 3D NOE Data: Change of Tertiary Structure upon Binding to the Lac Operator", J. Mol. Biol. 259 (1996), 761-773.

C.A.E.M. Spronk, M. Slijper, J.H. van Boom, R. Kaptein and R. Boelens, "The hinge helix in the lac repressor is induced upon binding to the lac operator", Nat. Struct. Biol. 3 (1996) 916-919.

F.A.A. Mulder, C.A.E.M. Spronk, M. Slijper, R. Kaptein and R. Boelens, "Improved HSQC experiments for th observation of exchange broadened signals", J Biomol. NMR 8 (1996) 223-228.

M. Cox, N. Dekker, R. Boelens, H.C. van Leeuwen, P.C. van der Vliet and R. Kaptein,
"A refined NMR solution structure of the POU-specific domain of the human Oct-1 protein",
In: Dynamics and the Problem of Recognition in Biological Macromolecues, Jaardetzky and Lefèvre (eds.), Plenum Press, New York, 1996, pp. 223-246.

H. Vis, O. Vageli, J. Nagel, C.E. Vorgias, K.S. Wilson, R. Kaptein and R. Boelens, "An NMR Study on the Interaction of the HU Protein from Bacillus stearothermophilus with DNA", Magn. Res. in Chem. 34 (1996) S81-S86.



R.M.A. Knegtel, M.A.A. van Tilborg, R. Boelens and R. Kaptein, "NMR Structural Studies on the Zinc Finger Domains of Nuclear Hormone Receptors", In: "Interface between Chemistry and Biochemistry". Ed. P. Jolles and H. Jörnvall, Birkhäuser Verlag, Basel, 1995, pp. 279-295.

M.J.M. Burgering, M. Hald, R. Boelens, J.N. Breg and R. Kaptein, "Hydrogen Exchange Studies of the Arc Repressor: Evidence for a Monomeric Folding Intermediate",  Biopolymers 35 (1995) 217-226.

R.M.A. Knegtel, R.H. Fogh, G. Ottleben, H. Rüterjans, P. Dumoulin, M. Schnarr, R. Boelens and R. Kaptein, "A Model for the LexA Repressor DNA Complex", Proteins 21 (1995) 226-236.

J.N. Breg, L. Sarda, P.J. Cozzone, R. Boelens and R. Kaptein, "Solution structure of porcine pancreatic procolipase as determined from 1H homonuclear 2D- and 3D-NMR experiments at 500- and 600-MHz",
Eur.J.Biochem. 227 (1995) 663-672.

E.C. van Geerestein-Ujah, M. Slijper, R. Boelens and R. Kaptein, "Graph-theoretical assignment of secondary structure in multi-dimensional protein NMR spectra. Application to lac repressor headpiece", J. Biomol. NMR 6 (1995) 67-78.

R.H. Fogh, D. Schipper, R. Boelens and R. Kaptein, "Complete 1H, 13C and 15N NMR assignments and secondary structure of the 269 residue serine protease PB92 from Bacillus alcalophilus" J. Biomol. NMR 5 (1995) 259-270

M. Cox, P.J.A. van Tilborg, W. de Laat, R. Boelens, H.C. van Leeuwen, P.C. van der Vliet, and R. Kaptein, "Solution structure of the Oct-1 POU-homeo domain determined by NMR and Restrained Molecular Dynamics", J. Biomol. NMR 6 (1995) 23-32.

B. van den Berg, M. Tessari, R. Boelens, R. Dijkman, R. Kaptein, G.H. de Haas and H.M. Verheij,
"Solution structure of porcine pancreatic phospholipase A2 complexed with micelles and a competitive inhibitor", J. Biomol. NMR 5 (1995) 110-121.

B. van den Berg, M. Tessari, R. Boelens, R. Dijkman, G.H. de Haas, R. Kaptein and H.M. Verheij,
"NMR structures of phospholipase A2 reveal conformational changes during interfacial activation",
Nature Structural Biology  (1995) 2 (5), 402-406

M.A.A. van Tilborg, A.M.J.J. Bonvin, K. Hård, A.L. Davis, B. Maler, R. Boelens, K.R. Yamamoto and R. Kaptein, "Structure Refinement of the Glucocorticoid Receptor-DNA Binding Domain from NMR Data by Relaxation Matrix Calculations", J. Mol. Biol. (1995) 247, 689-700.

B. van den Berg, M. Tessari, G.H. de Haas, H.M. Verheij, R. Boelens and R. Kaptein,
"Solution structure of porcine pancreatic phospholipase A2", The EMBO J 14 (1995) 4123-4131.

H. Vis, M. Mariani, C.E. Vorgias, K.S. Wilson, R. Kaptein and R. Boelens,
"Resonance Assignments of uniformly 13C/15N labeled proteins. Application to HU Protein from Bacillus staerothermophilus", Quart. Magn. Res. in Biol. Med. II(2) (1995) 107-117.

R. Kaptein, R. Boelens, V.P. Chuprina, J.A.C. Rullmann and M. Slijper, "NMR and nucleic acid-protein interaction: the lac repressor operator system", IN :Methods and Enzymology. Vol 261. Nuclear Magnetic Resonance and Nucleic Acids. Ed. T.L. James. Academic Press, San Diego 199, pp513-524

M. Slijper, A.M.J.J. Bonvin, R. Boelens and R. Kaptein,
"Application of Structure Refinement Using 3D NOE-NOE Spectroscopy to lac Repressor Headpiece (1-56)", J. Magn. Res. B 107 (1995) 298-301.

A.P.A.M. Eijkelenboom, R.A. Puras Lutzke, R. Boelens, R.H.A. Plasterk, R. Kaptein & K. Hård,
"The DNA-binding domain of HIV-1 integrase ihas an SH3-like fold", Nature Struct. Biol. 2 (1995) 807-810.

N.A.J. van Nuland, R. Boelens, R.M. Scheek and G.T. Robillard, "High-resolution Structure of the Phophorylated Form of the Histidine-containing Phosphocarrier Protein HPr from Escherichia coli Determined by Restrained Molecular Dynamics from NMR-NOE Data", J. Mol. Biol. 246 (1995) 180-193.

M. Tessari, M. Mariani, R. Boelens and R. Kaptein, "(H)XYH-COSY and (H)XYH-E. COSY Experiments for Backbone and Side-Chain Assignment and Determination of 3JHH' Couping Constants in (13C, 15N)-Labeled Proteins", J. Magn. Res. B 108 (1995) 89-93.

H. Vis, M. Mariani, C.E. Vorgias, K.S. Wilson, R. Kaptein and R. Boelens, "Solution Structure of the HU Protein from Bacillus stearothermophilus", J. Mol. Biol. 254 (1995), 692-703

L.P.A. van Houte, V.P. Chuprina, M. van der Wetering, R. Boelens, R. Kaptein and H. Clevers,
"Solution structure of the sequence-specific HMG box of the lymphocyte transcriptional activator Sox-4", J. Biol. Chem. 270 (1995) 30516-30524.

R. Kaptein, M. Slijper and R. Boelens, "Structure and dynamics of the lac repressor-operator complex as determined by NMR", In: Proceedings of the International Congress of Toxicology -VII, Ed. D.J. Reed, Elsevier Amsterdam, Toxicology Letters 82/83 (1995) 591-599.


L. Holm, C. Sander, H. Rüterjans , M. Schnarr, R. Fogh, R. Boelens,  and R. Kaptein,
"LexA repressor and iron-uptake regulator from E. coli: new members of the CAP-like DNA-binding domain superfamily", Protein Engineering 7 (1994) 1449-1453.

R.M.A. Knegtel, J.A.C. Rullmann, R. Boelens and R. Kaptein, "MONTY: A Monte Carlo approach to protein-DNA recognition", J. Mol. Biol. 235 (1994) 318-324.

M. Cox, J. Schaller, R. Boelens, R. Kaptein, E. Rickli and M. Llinás, "Kringle solution structures via NMR. Two-dimensional 1H-NMR analysis of horse plasminogen kringle 4", Chem. Physics of Lipids 67/68 (1994) 43-58.

A.M.J.J. Bonvin, R. Boelens and R. Kaptein, "Direct Nuclear Overhauser Effect Refinement of Crambin from Two-Dimensional NMR Data Using a Slow-Cooling Annealing Protocol", Biopolymers 34 (1994) 39-50.

A.M.J.J. Bonvin, H. Vis, J.N. Breg, M.J.M. Burgering, R. Boelens and R. Kaptein, "NMR solution structure of the Arc repressor using relaxation matrix calculations", J. Mol. Biol. 236 (1994) 328-341.

A.M.J.J. Bonvin, R. Boelens and R. Kaptein, "Time- and ensemble-averaged direct NOE restraints",     J. Biomol. NMR 4 (1994) 143-149.

R. Boelens, M. Burgering, R.H. Fogh and R. Kaptein, "Time-saving methods for heteronuclear multidimensional NMR of (13C, 15N) doubly-labeled proteins", J. Biomol. NMR 4 (1994) 201-213.

R.H. Fogh, D. Schipper, R. Boelens and R. Kaptein, "1H, 13C, and 15N NMR backbone assignments of the 269 residue serine protease PB92 from Bacillus alcalophilus", J. Biomol. NMR 4 (1994) 123-128.

R.M.A. Knegtel, R. Boelens and R. Kaptein, "Monte Carlo Docking of Protein-DNA Complexes: Incorporation of DNA Flexibility and Experimental Data", Protein Engineering 7 (1994) 761-767.

R. Kaptein, R. Boelens, V.P. Chuprina and J.A.C. Rullmann, "NMR Studies of Protein-Nuclein Acid Interaction: The Lac Operon", In: "NMR of Biological Macromolecules", Ed.  C.I. Stassinopoulou, Nato ASI Series, Vol H 87, Springer-Verlag Berlin, 1994, pp. 223-333.

T. de Beer, C.W.E.M. van Zuylen, K. Hård, R. Boelens, R. Kaptein, J.P. Kamerling and J.F.G. Vliegenthart, "Rapid and simple approach for the NMR resonance assignment of the carbohydrate chains of an intact glycoprotein. Application of gradient-enhanced natural abundance 1H-13C HSQC and HSQC-TOCSY to the -subunit of human chorionic gonadotropin", FEBS Lett. 348 (1994) 1-6.

M. Mariani, M. Tessari, R. Boelens, H. Vis and R. Kaptein, "Assignment of the protein backbone from a single 3D 15N, 13C time-shared HXYH experiment",  J. Magn. Res., Series B. 104 (1994) 294-297.

M.J.M. Burgering, R. Boelens, D.E. Gilbert, J.N. Breg, K.L. Knight, R.T. Sauer and R. Kaptein,
"Solution Structure of Dimeric Mnt Repressor (1-76)", Biochemistry 33 (1994), 15036-15045.

R.H. Fogh, G. Ottleben, H. Rüterjans, M. Schnarr, R. Boelens and R. Kaptein, "Solution Structure of the LexA Repressor DNA Binding Domain, Determined by 1H NMR Spectroscopy", EMBO J. 13 (1994) 3936-3944.    

W.D. Hoff, P. Düx, B. Devreese, I.M. Nugteren-Roodzand, W. Crielaard, R. Boelens, R. Kaptein, J. Van Beeumen and K.J. Hellingwerf, "Thiol ester-linked p-coumaric acid as a new photoactive cofactor in a rhodopsin-like protein", Biochemistry 33 (1994) 13959-13962.

H. Vis, R. Boelens, M. Mariani, R. Stroop, C.E. Vorgias, K.S. Wilson and R. Kaptein, "1H, 13C and 15N Resonance Assignments and Secondary Structure Analysis of the HU Protein from Bacillus stearothermophilus Using Two- and Three-Dimensional Double- and Triple-Resonance Heteronuclear Magnetic Resonance Spectroscopy", Biochemistry 33 (1994) 14858-14870.


J.A.C. Rullmann, A.M.J.J. Bonvin, R. Boelens and R. Kaptein, "Structure determination form NMR - Application to crambin", In: "Computation of Biomolecular Structures" Eds. D.M. Soumpasis and T.M. Jovin, Springer Verlag New York  1993, pp. 1-14.

R.M.A. Knegtel, M. Katahira, J.G. Schilthuis, R. Boelens, D. Eib, P.T. van der Saag and R. Kaptein, "The solution strucure of the human retinoic acid receptor-? DNA-binding domain", J. Biomol. NMR 3  (1993) 1-17.

A.M.J.J. Bonvin, J.A.C. Rullmann, R.M.J.N. Lamerichs, R. Boelens and R. Kaptein,
"'Ensemble' Iterative Relaxation Matrix Approach: a new NMR refinement protocol applied to the solution structure of crambin", Proteins 15 (1993) 385-400.

R.M.A. Knegtel, M. Katahira, J.G. Schilthuis, R. Boelens, D. Eib, P.T. van der Saag and R. Kaptein
"Three-dimensional structure of the human retinoic acid receptor-? DNA-binding domain: implications for DNA binding", In: "New Developments in Lipid-Protein Interaction and Receptor Function"
Ed. K.W.A. Wirtz et al., Plenum Press, New York, 1993, pp.153-168

G.J.A. Kleywegt, G.W. Vuister, A. Padilla, R.M.A. Knegtel, R. Boelens and R. Kaptein, "Computer-Assisted Assignment of Homonuclear 3D spectra of Proteins. Application to Pike Parvalbumin III",     J. Magn. Reson. 102, 166-176

R.M.A. Knegtel, R. Boelens, M.L. Ganadu, A.V.E. George, M. Katahira, A.M.J.J. Bonvin, D. Eib, P.T. van der Saag and R. Kaptein, "NMR studies of the human retinoic acid receptor-DNA-binding domain: metal coordination and three dimensional structure", In: "Zinc Finger Proteins in Ocogenesis. DNA-Binding and Gene Regulation", Ed. M. Sluyser, G. Ab, A.O. Brinkmann and R.A. Blankenstein, Annals of the Academy of Sciences 684 (1993) 49-62.

N. Dekker, M. Cox, R. Boelens, C.P. Verrijzer, P.C. van der Vliet and R. Kaptein, "The solution structure of the POU-specific DNA binding domain of Oct-1", Nature 362 (1993), 852-855.

M. Cox, N. Dekker, R. Boelens, C.P. Verrijzer, P.C. van der Vliet and R. Kaptein, "NMR studies of the POU-specific DNA-binding domain of Oct-1: sequential 1H and 15N assignments and secondary structure", Biochemistry 32 (1993), 6032-6040.

R.M.A. Knegtel, R. Boelens, M.L. Ganadu, A.V.E. George, P.T. van der Saag and R. Kaptein,
"Heteronuclear 113Cd-1H NMR study of metal coordination in the human retinoic acid receptor-? DNA binding domain, Biochem. Biophys. Res. Com. 192 (1993) (2), 492-498.

V.P. Chuprina, J.A.C. Rullmann, R.M.J.N. Lamerichs, J.H. van Boom, R. Boelens and R. Kaptein,
"Structure of the Complex of lac Repressor Headpiece and an 11 Base Pair Half-Operator determined by NMR Spectroscopy and Restrained Molecular Dynamics", J. Mol. Biol. 234 (1993) 446-462.

M.J.M. Burgering, R. Boelens, M. Caffrey, J.N. Breg and R. Kaptein, "Observation of inter-subunit Nuclear Overhauser Effects in a dimeric protein: Application to the Arc repressor", FEBS Lett.330 (1993) 105-109.

M.J.M. Burgering, R. Boelens and R. Kaptein, "Observation of inter-subunit NOE's in a dimeric P232 Mnt repressor mutant by a time-shared [15N, 13C] double half-filter technique", J. Biomol. NMR 3 (1993) 709-714.

A.M.J.J. Bonvin, R. Boelens and R. Kaptein, "Determination of biomolecular structures by NMR. Use of relaxation matrix calculations",  In: "Computer Simulation of Biomolecular Systems". Vol. 2. Eds: W.F. van Gunsteren, P.K. Weiner and R.J. Wilkinson, Escom Leiden 1993, pp. 407-440.

1992 Waard, B.R.Leeflang,  J.F.G.Vliegenthart., R.Boelens, G.W. Vuister  and R.Kaptein,
"Application of 2D and 3D NMR experiments to the conformational study of a diantennary oligosaccharide", J. Biomol. NMR 2 (3) (1992) 211-226.

G.W. Vuister, R.Boelens, R.Kaptein, M. Burgering and P. C.M. van Zijl, "Gradient-Enchanced 3D NOESY-HMQC Spectroscopy", J. Biomol. NMR 2 (3) (1992) 301-305.

M. Katahira, R.M.A. Knegtel, R. Boelens, D. Eib, J.G. Schilthuis, P.T. van der Saag and R. Kaptein, "Homo- and heteronuclear NMR studies of the human retinoic acid receptor-? DNA binding domain: sequential assignments and secondary structure elements", Biochemistry 31, 6474-6480

E.R. Kellenbach, M.L. Remerowski, D. Eib, R. Boelens, G.A. van der Marel, H. van der Elst, J.H. van Boom en R. Kaptein, "Synthesis of Isotope Labeled Ologonucleotides and Their Use in an NMR Study of a Protein-DNA Complex", Nucl. Acids Res. 20 (4) (1992) 653-657.

A.L. Davis, R. Boelens and R. Kaptein, "Coherence transfer selection in three-dimensional triple-resonance experiments by pulsed field gradient techniques", J. Biomol. NMR 2 (1992) 395-400.

M.L. Ganadu, F. Bonomi, S. Pagani, R. Boelens, "1H NMR Studies on the Oxidized Ferredoxin from Colostridium pasteurianum", Biochemistry International 26 (4) (1992) 577-585.

A.R. Peters, N. Dekker, L. van den Berg, R. Boelens, R. Kaptein, A.J. Slotboom en G.H. de Haas,
"Conformational Changes in Phospholipase A2 upon Binding to Micellar Interfaces in the Absence and Presence of Competitive Inhibitors. A 1H and 15N NMR Study", Biochemistry 31 (1992) 10024-10030


N. Dekker, A.R. Peters, A.J. Slotboom, R. Boelens, R. Kaptein and G. de Haas,
"Porcine Pancreatic Phospholipase A2: Sequence-Specific 1H and 15N NMR Assignments and Secondary Structure", Biochemistry,  30 (1991) 3135-3146.

N. Dekker, A.R. Peters, A.J. Slotboom, R. Boelens, R. Kaptein, R. Dijkman and G. de Haas,
"1H 2D NMR studies of phospholipase A2-inhibitor complexes bound to a micellar lipid-water interphase", Eur. J. Biochem. 199 (1991) 601-607.

C. Gonzalez, J.A.C. Rullmann, A.M.J.J. Bonvin, R. Boelens and R. Kaptein, "Towards an NMR R-factor" J. Magn. Reson. 91 (1991) 659-664.

R. Kaptein, R. Boelens and T.M.G. Koning, "NMR studies of proteins, nucleic acids and their interactions", In: "NMR and biomolecular structure" Eds. I. Bertini, H. Molinari and N. Nicolai, VCH Weinheim, 1991, pp.113-139.

G.J. Kleywegt, R. Boelens, M. Cox, M. Llinás, and R. Kaptein, "Computer-assisted assignment of 2D 1H NMR spectra of proteins. Basic algorithms and application to phoratoxin B", J. Biomol. NMR,  1 (1991)  23-47.

E. Kellenbach, T. Härd, R. Boelens, K. Dahlman, J. Carlstedt-Duke, J.-Å. Gustafsson, G.A. van der Marel, J.H. van Boom, B. Maler, K.R. Yamamoto, and R. Kaptein, "Photo-CIDNP Study of the Interaction between the Glucocorticoid Receptor DNA-binding Domain and Glucocorticoid Response Elements", J. Biomol. NMR, 1 (1991) 105-110.

 T.M.G. Koning, R. Boelens, G.A. van der Marel, J.H. van Boom and R. Kaptein,
"Structure determination of a DNA octamer in solution by NMR spectroscopy. The effect of fast local motions", Biochemistry, 30 (1991) 3787-3797.

E. Kellenbach, H. van den Elst, R. Boelens, G.A. van der Marel, J.H. van Boom en R. Kaptein, "A convenient synthesis of DNA fragments nitrogen-15 labeled at the exocyclic cytosine amino group",
Recl. Trav. Chim. Pays-Bas, 110 (1991), 9, 387-388.

G.W. Vuister, R.Boelens, R.Kaptein, R.E. Hurd, B.J. and P.C.M. van  Zijl, "Gradient-Enhanced HMQC and HSQC Spectroscopy. Applications to 15N-labelled Mnt Repressor", J. Am. Chem. Soc. 133 (1991) 9688-9690.

E. Kellenbach, B.A. Maler, K.R. Yamamoto, R.Boelens  and R. Kaptein, "Identification of the Metal Coordinating Residues in the DNA Binding Domain of the Glucocorticoid Receptor by 113Cd-1H Heteronuclear NMR spectroscopy", FEBS Lett. 291 (1991), 2, 367-370.

A.M.J.J. Bonvin, R. Boelens and R. Kaptein, "Direct NOE refinement of biomecular structures using 2D NMR data", J. Biomol. NMR, 1 (1991) 305-309.

R.M.A. Knegtel, R. Boelens, M.L. Ganadu and R.Kaptein, "The solution structure of a monomeric insulin. A 2D 1H-NMR study of des-pentapeptide-insulin in combination with distance geometry and restrained molecular dynamics", Eur. J. Biochem. 202 (1991) 447-458.

G.W. Vuister, R. Boelens, A. Padilla and R. Kaptein, "Statistical Analysis of Double NOE Transfer Pathways in Proteins as Measured in 3D NOE-NOE Spectroscopy", J. Biomol. NMR 1 (1991) 421-438.

M.L. Remerowski, E. Kellenbach, R. Boelens, G.A. van der Marel, J.H. van Boom, B.A. Maler, K.R. Yamamoto and R. Kaptein, "1H-NMR Studies of DNA Recognition by the Glucocorticoid Receptor: Complex of the DNA Binding Domain with a Half-Site Response Element", Biochemistry 30 (1991) 11620-11624.

Gerard J. Kleywegt, Rolf Boelens and Robert Kaptein, "STELLA and CLAIRE: A Seraglio of Programs for Human-Aided Assignment of 2D 1H NMR Spectra of Proteins", In: "Computational Aspects of the Study of Biological macromolecules by Nuclear Magnetic Resonance Spectroscopy", Ed. J.C. Hoch et al., Plenum Press, New York,  1991, pp. 427-438.

R. Kaptein, T.M.G. Koning and R. Boelens, "How to Deal with Spin-Diffusion and Internal Mobility in Biomolecules. A Relaxation Matrix Approach", In: "Computational Aspects of the Study of Biological macromolecules by Nuclear Magnetic Resonance Spectroscopy", Ed. J.C. Hoch et al., Plenum Press, New York, 1991, pp . 349-360.

Rolf Boelens, Christian Griesinger, Lewis E. Kay, Dominique Marion, and Erik R.P. Zuiderweg
"Applicability and Limitations of Three-Dimensional NMR Spectroscopy for the Study of Proteins in Solution", In: "Computational Aspects of the Study of Biological macromolecules by Nuclear Magnetic Resonance Spectroscopy", Ed. J.C. Hoch et al., Plenum Press, New York, 1991, pp. 127-150.

A.M.J.J. Bonvin, R. Boelens and R.Kaptein, "Direct Structure Refinement using, 3D NOE-NOE Spectra of Biomolecules", J. Magn. Reson. 95 (1991) 626-631. 


R. Boelens, G.W. Vuister, A. Padilla, G.J. Kleywegt, P. de Waard, T.M.G. Koning and R. Kaptein,
"Three-dimensional NMR spectroscopy of biomolecules", In "Structure & Methods, DNA Protein Complexes & Proteins",  Proceedings of the Sixth Conversation in Biomolecular Stereodynamics, Eds. R.H. Sarma and M.H. Sarma,  Adenine Press, Volume 2, 1990, pp.63-81.
G.W. Vuister, R. Boelens, A. Padilla, G.J. Kleywegt and R. Kaptein, "Assignment strategies in homonuclear three-dimensional 1H NMR spectra of proteins", Biochemistry,  29 (1990) 1829-1839.
J.A.C. Rullmann,  R. Boelens, R.M.J.N. Lamerichs, G.W. Vuister and R. Kaptein, "NMR studies of proteins and protein-DNA interactions", In "Modelling of Molecular Structures and Properties",  Proceedings of the 44th International Meeting of Physical Chemistry, Nancy, France, Ed. J.L. Rivail, Elsevier, Amsterdam, Volume 71, 1990, pp. 661-678.

"Structure determination from NMR using a relaxation matrix approach; application to the solution structure of crambin", In "Modelling of Molecular Structures and Properties", Proceedings of the 44th International Meeting of Physical Chemistry, Studies in Physical and Theoretical Chemistry, Volume 71, Ed. J.L. Rivail, Elsevier, Amsterdam, 1990, pp.703-710.

P. de Waard, R. Boelens, G.W. Vuister and J.F.G. Vliegenthart, "Structural studies of oligosaccharides by 1H/13C 2D and 3D HMQC-NOE at natural abundance", J. Am. Chem. Soc. 112 (1990) 3232-3234.

R. Kaptein, R.M.J.N. Lamerichs, R. Boelens and J.A.C. Rullmann, "Two-dimensional NMR study of a protein-DNA complex. Lac repressor headpiece-operator interaction", Biochemical Pharmacology, 40 (1990) 89-96.

R. Boelens, M.L. Ganadu, P. Verheyden and R. Kaptein, "2D NMR studies on des-pentapeptide-insulin. Proton resonance assignments and secondary structure analysis", Eur. J. Biochemistry, 191 (1990) 147-153.

G.J. Kleywegt, R. Boelens and R. Kaptein, "A versatile approach towards the (partially) automatic recognition of cross peaks in 2D 1H NMR spectra", J. Magn. Reson.  88 (1990) 601-608.

A. Padilla, G.W. Vuister, R. Boelens, G.J. Kleywegt, A. Cavé, J. Parello and R. Kaptein,
"Homonuclear  three-dimensional 1H-NMR spectroscopy of pike parvalbumin. Comparison of short- and medium-range NOEs from 2D and 3D NMR", J. Am. Chem. Soc.  112 (1990) 5024-5030.

R. Kaptein,   R.M.J.N. Lamerichs,   R. Boelens,  A. Padilla,   H. Rüterjans   and M. Schnarr, "The helix-turn-helix subdomains of LexA and Lac repressors, In: "Frontiers of NMR in Molecular Biology", UCLA Symposia on Molecular and Cellular Biology, New Series, Vol. 109, Eds. D. Live, I. Armitage & D. Patel, Alan R. Liss, Inc., New York, pp. 119-127, 1989.

T.M.G. Koning, R. Boelens and R. Kaptein, "Calculation of the Nuclear Overhauser Effect and the determination of proton-proton  distances in the presence of internal motions", J. Magn. Reson., 90 (1990) 111-123.

J.N. Breg, R. Boelens, G.W. Vuister and R. Kaptein, "3D NOE-NOE spectroscopy of proteins. Observation of sequential 3D NOE cross peaks in Arc repressor", J. Magn. Reson., 87 (1990) 646-651.

J.A.C. Rullmann, R. Boelens en R. Kaptein, "De struktuur van een eiwit-DNA complex in oplossing. De nieuwe mogelijkheden van NMR", Chemisch Magazine (1990) 131-133.

G. Vuister, R. Boelens en R. Kaptein,
"3D NMR: nieuwe dimensie in structuuronderzoek", Chemisch Magazine  (1990) 79-83.
 T. Härd, E. Kellenbach, R. Boelens, B.A. Maler, K. Dahlman, L.P. Freedman, J. Carlstedt-Duke, K.R. Yamamoto, J.-Å. Gustafsson and R. Kaptein, "Solution Structure of the Glucocorticoid Receptor DNA-Binding Domain", Science, 249 (1990) 157-160.

T. Härd, E. Kellenbach, R. Boelens, K. Dahlman, J. Carlstedt-Duke, L.P. Freedman, B.A. Maler, E.I. Hyde, J.-Å. Gustafsson, K.R. Yamamoto and R. Kaptein,  "1H-NMR studies of the glucocorticoid receptor DNA-binding domain: sequential assignments and identification of secondary structure elements", Biochemistry, 29 (1990) 9015-9023.

J.N. Breg, J.H.J. van Opheusden, M.J.M. Burgering, R. Boelens and R. Kaptein,
"The structure of Arc repressor in solution. A family of ?-sheet DNA-binding proteins"
Nature, 346 (1990) 586-589.

R.M.J.N. Lamerichs, R. Boelens, G.A. van der Marel, J.H. van Boom and R. Kaptein,
"Assignment of the 1H-NMR spectrum of a lac repressor headpiece-operator complex in H2O and identification of NOEs", Eur. J. Biochem., 194 (1990) 629-637.


S. Kosasi, W.G. van der Sluis, R. Boelens, L.A. 't Hart and R.P. Labadie, "Labaditin, a novel cyclic decapeptide from the latex of jatropha multifida L.(Euphorbiaceae)", FEBS Letters  256 (1989) 91-96.

G.W. Vuister, P. de Waard, R. Boelens, J.F.G. Vliegenthart and R. Kaptein, "The use of 3D NMR in structural studies of oligosaccharides", J. Am. Chem. Soc., 111  (1989)  772-774.

R. Kaptein, R. Boelens and R.M.J.N. Lamerichs, "NMR studies of protein-DNA recognition. The interaction of lac repressor headpiece with operator DNA", In: "Protein-Nucleic Acid Interaction"
Eds. W. Saenger and U. Heinemann, Mac Millan Press, London, Vol.10  (1989), pp.35-59.

R. Kaptein, R. Boelens and J.A.C. Rullmann, "Biomolecular structures from NMR. Computational aspects", In: "Computer simulation of biomolecular systems", Theoretical and experimental applications.
Eds. W.F. van Gunsteren and P.K. Weiner, ESCOM Science Publishers B.V., Leiden, pp. 194-216, 1989.

R. Boelens, T.M.G. Koning, G.A. van der Marel, J.H. van Boom and R. Kaptein,
"Iterative procedure for structure determination from proton-proton NOE's using a full relaxation matrix approach. Application to a DNA octamer", J. Magn. Reson., 82  (1989) 290-308.

S. Stob, R.M. Scheek, R. Boelens, K. Dijkstra and R. Kaptein, "Applications of 2D 1H NMR methods to Photo-CIDNP Spectroscopy", Israel J. Chem., 28 (1989) 319-327.

J.A.C. Rullmann, R. Boelens and R. Kaptein, "NMR based docking studies of lac repressor headpiece on a lac operator fragment", In "DNA-Protein Interactions in Transcription", UCLA Symposia on Molecular and Cellular Biology, New Series, Vol. 95, Ed. J.D. Gralla. Alan R. Liss, Inc., New York, pp. 11-24 , 1989.
A. De Marco, A.M. Petros, M. Llinás, R. Kaptein and R. Boelens, "Ligand-binding effects on the kringle 4 domain from human plasminogen: a study by laser photo-CIDNP 1H-NMR spectroscopy", Biochim. Biophys. Acta, 994 (1989) 121-137.

R.M.J.N. Lamerichs, R. Boelens, G.A. van der Marel, J.H. van Boom, R. Kaptein, F. Buck, B. Fera and H. Rüterjans, "1H NMR study of a complex between lac  repressor headpiece and a 22 base pair symmetric lac operator", Biochemistry, 28  (1989) 2985-2991.

J. Fisher, W.U. Primrose, G.C.K. Roberts, N. Dekker, R. Boelens, R. Kaptein and A.J. Slotboom,
"1H NMR studies of bovine and porcine phospholipase A2: assignment of aromatic resonances and evidence for a conformational equilibrium in solution", Biochemistry, 28 (1989) 5939-5946.

R.M.J.N. Lamerichs, A.Padilla, R. Boelens, R. Kaptein, G. Ottleben, H. Rüterjans, M. Granger-Schnarr, P. Oertel and M. Schnarr, "The amino-terminal domain of LexA repressor is ?-helical but differs from canonical helix-turn-helix proteins: A two-dimensional 1H NMR study", Proc. Natl. Acad. Sci. USA, 86 (1989) 6863-6867.

K.H. Mayo, R. Cavalli, A.R. Peters, R. Boelens and R. Kaptein, "Sequence - Specific 1H-NMR Assignments and Peptide Backbone Conformation in Rat Epidermal Growth Factor", Biochem. J., 257 (1989) 197-205.

J.N. Breg, R. Boelens, A.V.E. George and R. Kaptein, "Sequence-Specific 1H NMR assignment and secondary structure of the arc repressor of bacteriophage P22, as determined by two-dimensional 1H NMR spectroscopy" Biochemistry 28 (1989) 9826-9833.

G.J. Kleywegt, R.M.J.N. Lamerichs, R. Boelens and R. Kaptein, "Towards automatic assignment of protein 1H NMR spectra", J. Magn. Reson. 85, (1989) 186-197.

R. Boelens, G.W. Vuister, T.M.G. Koning and R. Kaptein, "The observation of spin-diffusion in biomolecules by 3D NOE-NOE spectroscopy", J. Am. Chem. Soc. 111 (1989) 8525-8526.


R.M.J.N. Lamerichs, L.J. Berliner, R. Boelens, A. De Marco, M. Llinàs en R. Kaptein,  "Secondary structure and hydrogen bonding of crambin in solution. A two-dimensional NMR study", Eur. J. Biochem., 171 (1988) 307-312.

H. Pepermans, D. Tourwé, G. van Binst, R. Boelens, R.M. Scheek, W.F. van Gunsteren en R. Kaptein, 
"The Combined Use of NMR, Distance Geometry, and Restrained Molecular Dynamics for the Conformational Study of a Cyclic Somatostatin Analogue",  Biopolymers, 27 (1988) 323-338.

J.J.H. Nusselder, J.B.F.N. Engberts, R. Boelens en R. Kaptein, 
"Micellar structure studied by 2D-NMR",  Recl. Trav. Chim. Pays-Bas, 107 (1988) 105-107. 

R. Boelens, T.M.G. Koning and R. Kaptein, "Determination of biomolecular structures from proton-proton NOE's using a relaxation matrix approach", J. Mol. Structure, 173 (1988) 299-311.

R. Kaptein and R. Boelens, "NMR studies of repressor-operator interaction. The lac control region",
    In "Nucleic Acids and Molecular Biology", Vol. 2,  Eds. F. Eckstein and D.M.J. Lilley, Springer-Verlag, Berlin,  Heidelberg, 1988, pp. 167-187.

G.W. Vuister, R. Boelens and R. Kaptein, "Non-selective three-dimensional NMR spectroscopy. The 3D NOE-HOHAHA experiment", J. Magn. Reson., 80  (1988) 176-185.

R. Kaptein, R. Boelens, R.M. Scheek and W.F. van Gunsteren, "Protein structures from NMR", Biochemistry, 27 (1988) 5389-5395.

K.H. Mayo, A. Schussheim, G.W. Vuister, R. Boelens, R. Kaptein, M. Engelhard and B. Hess, "Mobility and solvent exposure of aromatic residues in bacteriorhodopsin investigated by 1H-NMR and photo-CIDNP-NMR spectroscopy", FEBS Letters, 235 (1988) 163-168.

S. Stob, R.M. Scheek, R. Boelens and R. Kaptein, "Photo-CIDNP study of the interaction between lac repressor headpiece and lac operator DNA", FEBS Letters, 239 (1988) 99-104.

R. Boelens, R.M.J.N. Lamerichs, J.A.C. Rullmann, J.H. van Boom and R. Kaptein, "The interaction of lac repressor headpiece with its operator. An NMR view", Protein Seq. Data Anal., 1 (1988) 487-498.


J. Kemmink, R. Boelens, T. Koning, R. Kaptein, G.A. van der Marel and J.H. van Boom,"Conformational changes in the oligonucleotide duplex d(GCGTTGCG). d(CGCAACGC) induced by formation of a cis-syn  thymine dimer, A two-dimensional NMR study",  Eur. J. Biochem, 162 (1987) 37-43.

J. Kemmink, R. Boelens and R. Kaptein,  "Two-dimensional 1H-NMR study of two cyclobutane type photodimers of thymidylyl-(3'?5')-thymidine",  Eur. Biophys. J., 14 (1987) 293-299.

R. Boelens, R.M. Scheek, J.H. van Boom and R. Kaptein,  "Complex of lac repressor Headpiece with a 14 base-pair lac operator fragment studied by two-dimensional nuclear magnetic resonance",  J. Mol. Biol., 193 (1987) 213-216.

J.A.W.H. Vermeulen, R.M.J.N. Lamerichs, L.J. Berliner, A. De Marco, M. Llinás, R. Boelens, J. Alleman and R. Kaptein,  "1H-NMR characterization of two crambin species",  FEBS Letters, 219 (1987) 426-430.

G.W. Vuister and R. Boelens,  "Three-Dimensional J-Resolved NMR Spectroscopy",  J. Magn. Reson., 73 (1987) 328-333.

J. Kemmink, R. Boelens, T. Koning, G.A. van der Marel, J.H. van Boom and R. Kaptein, 
"1H-NMR study of the exchangeable protons of the duplex d(GCGTTGCG). d(CGCAACGC) containing a thymine photodimer",  Nucleic Acids Res., 15, (1987) 4645-4653.

J. Lautz, H. Kessler, R. Boelens, R. Kaptein and W.F. van Gunsteren, "Conformational analysis of a cyclic thymopoietin - analogue by 1H NMR spectroscopy and restrained molecular dynamics simulations",  Int. J. Pept. Prot. Res., 30 (1987) 404-414.

R. Boelens, R.M. Scheek, R.M.J.N. Lamerichs, J. de Vlieg, J.H. van Boom and R. Kaptein, 
"A two-dimensional NMR study of the complex of lac repressor headpiece with a 14 base pair lac  operator fragment",  In "DNA-ligand Interactions. From Drugs to Proteins",  
Eds. W. Guschlbauer and W. Saenger, Plenum Press, New York, 1987, pp. 191-215


R. Wever, R. Boelens and A.C.F. Gorren, "The effect of pH on electron redistributions in cytochrome c oxidase", Frontiers in Bioinorganic Chemistry, Ed.: A.V. Xavier, VCH, Verlaggesellschaft, Weinheim, 1986, pp. 714-718.

J. Kemmink, G.W. Vuister, R. Boelens, K. Dijkstra and R. Kaptein,  "Nuclear spin coherence transfer in photochemical reactions",  J. Am. Chem. Soc., 108 (1986) 5631-5633.

R. Boelens, A. Podoplelov and R. Kaptein,  "Separation of net polarization and multiplet effect in coupled spin systems by two-dimensional CIDNP",  J. Magn. Res., 69 (1986) 116-123.

R.S. Norton, L. Beress, S. Stob, R. Boelens and R. Kaptein,  "Photochemically induced dynamic nuclear polarisation NMR study of the aromatic residues of sea-anemone polypeptide cardiac stimulants",  Eur. J. Biochem., 157 (1986) 343-346.

A. De Marco, L. Zetta, A.M. Petros, M. Llinás, R. Boelens and R. Kaptein, "Kringle 4 from human plasminogen: A proton Magnetic Resonance study via two-dimensional photochemically induced dynamic nuclear polarization spectroscopy", Biochemistry, 25 (1986) 7918-7923.

J. de Vlieg, R. Boelens, R.M. Scheek, R. Kaptein and W.F. van Gunsteren, "Restrained molecular dynamics procedure for protein tertiary structure determination from NMR data: A lac  repressor headpiece structure based on information on J-coupling and from presence and absence of NOE's", 
Israel J. of Chem., 27 (1986) 181-188.


E.R.P. Zuiderweg, M. Billeter, R. Kaptein, R. Boelens, R.M. Scheek and K. Wüthrich, "Solution Conformation of E.coli lac repressor DNA binding domain by 2D NMR: sequence location and spatial arrangement of three ?-helices", In: Prog. Bioorg. Chem. Mol. Biol., Ed: Y. Ovchinnikov, Elsevier, Amsterdam, 1985, 65-70.

R.M. Scheek, S. Stob, R. Boelens, K. Dijkstra and R. Kaptein,
"Applications of Two-dimensional NMR Methods in Photochemically Induced Dynamic Nuclear Polarization Spectroscopy", J. Am. Chem. Soc., 107, 1985, 705-706.

R. Kaptein, E.R.P. Zuiderweg, R.M. Scheek, R. Boelens and W.F. v. Gunsteren
"A Protein Structure from Nuclear Magnetic Resonance Data lac Repressor Headpiece",
J. Mol. Biol., 182, 1985, 179-182.

R.M. Scheek, R. Boelens, N. Russo and R. Kaptein, "Sequential Resonance Assignments in the 1H NMR Spectrum of a lac Operator Fragment by Two-dimensional NOE Spectroscopy at 500 MHz", In: "Structure & Motion: Membranes, Nucleic Acids & Proteins", Eds. E. Clementi, G. Corongiu, M.H. Sarma and R.H. Sarma, Adenine Press, 1985.

E.R.P. Zuiderweg, R. Boelens and R. Kaptein, "Stereospecific Assignments of 1H-NMR Methyl Lines and Conformation of Valyl Residues in the lac Repressor Headpiece", Biopolymers, 24, 1985, 601-611.

R.M. Scheek, E.R.P. Zuiderweg, R. Boelens, W.F. van Gunsteren and R. Kaptein
"The Tertiary Structure of the Lac Repressor Headpiece Derived from Nuclear Magnetic Resonance Spectroscopy", In: "Magnetic Resonance in Biology and Medicine",
Eds. G. Govil, C.L. Khetrapal and A. Saran, McGraw-Hill Publ. Comp. Ltd., New Delhi, 1985, 293-303.

R. Boelens, P. Gros, R.M. Scheek, J.A. Verpoorte and R. Kaptein, "Hydrogen Exchange of Individual Amide Protons in the E.Coli lac Repressor DNA-binding Domain: A Nuclear Magnetic Resonance Study (29)", J. Biomol. Struct. Dyn., 3, 1985, 269-280.

R. Boelens, R.M. Scheek, K. Dijkstra and R. Kaptein, "Sequential Assignment of Imino- and Amino-Proton Resonances in 1H NMR Spectra of Oligonucleotides by Two-Dimensional NMR Spectroscopy. Application to a lac Operator Fragment", J. Magn. Reson., 62, 1985, 378-386.

E.R.P. Zuiderweg, R.M. Scheek, R. Boelens, W.F. van Gunsteren and R. Kaptein,
    "Determination of protein structures from nuclear magnetic resonance data using a restrained molecular dynamics approach: The lac repressor DNA binding domain", Biochimie, 67, 1985, 707-715.

W.F. van Gunsteren, R. Boelens, R. Kaptein, R.M. Scheek and E.R.P. Zuiderweg, "An Improved Restrained Molecular Dynamics Technique to obtain Protein Tertiary Structure from Nuclear Magnetic Resonance Data", In "Molecular Dynamics and Protein Structure", Ed. J. Hermans, 1985, 92-99.

H. Kessler, B. Kutscher, R. Kerssebaum, A. Klein, J. Lautz, W.F. van Gunsteren, R. Boelens and R. Kaptein, "Design, synthesis, and conformation of superactive thymopoietin-analogues", In "Peptides: Structure and Function. Proc. Ninth American Peptide Symposium.", Eds. C.M. Deber, V.J. Hruby and K.D. Kopple. Pierce Chemical Company, 1985, 83-92.

R. Wever, R. Boelens, E. de Boer, B.F. van Gelder, A.C.F. van Gorren and H. Rademaker,
"The photoreactivity of copper - NO complexes in cytochrome c oxidase and in other copper - containing enzymes, J. Inorg. Biochem., 23, 1985, 227-232.

R. Wever, A.C.F. Gorren and R. Boelens, "Electron transfer reactions in cytochrome c oxidase", Rev. Port. de Quim.,  27, 1985, 148-149.


E.R.P. Zuiderweg, M. Billeter, R. Boelens, R.M. Scheek, K. Wüthrich and R. Kaptein, "Spatial arrangement of the three ?-helices in the solution conformation of E.coli  lac repressor DNA-binding domain", FEBS Letters, 174, 1984, 243-247.

R.M. Scheek, R. Boelens, N. Russo, J.H. van Boom and R. Kaptein, "Sequential Resonance Assignments in 1H NMR Spectra of Oligonucleotides by Two-dimensional NMR Spectroscopy", Biochemistry, 23, 1984, 1371-1376.

R.M. Scheek, S. Stob, R. Boelens, K. Dijkstra and R. Kaptein, "Applications of Two-dimensional 1H Nuclear Magnetic Resonance Methods in Photochemically Induced Dynamic Nuclear Polarization Spectroscopy", Faraday Discuss. Chem. Soc., 78, 1984, 245-256.

C.T.W. Moonen, R.M. Scheek, R. Boelens and F. Müller, "The use of 2D NMR spectroscopy and 2D difference spectra in the elucidation of the active center of Megasphaera elsdenii flavodoxin", Eur. J. Biochem. 141, 1984, 323-330.

R. Boelens, H. Rademaker, R. Wever and B.F. van Gelder, "The cytochrome c oxidase-azide-nitric oxide complex as a model for the oxygen binding site", Biochim. Biophys. Acta  765, 1984, 196-209.

R. Boelens, "Ligand binding to and electron transfer in cytochrome c oxidase",
Ph.D. Thesis, University of Amsterdam, Dijkstra Niemeyer, Groningen.


R. Boelens, R. Wever, B.F. van Gelder and H. Rademaker, "An ERP study of the photodissociation reactions of oxidised cytochrome c oxidase-nitric oxide complexes", Biochim. Biophys. Acta  724, 1983, 176-183.
R. Kaptein, R.M. Scheek, E.R.P. Zuiderweg, K.J.M. Klappe, R. Boelens, J.H. van Boom, H. Rüterjans and K. Beyreuther, "NMR Studies on the Interaction of the E. Coli Lac Repressor with Lac Operator DNA", In "Structure and Dynamics: Nucleic Acids and Proteins", Eds. E. Clementi and R.H. Sarma, Adenine Press, N.Y., 1983, 209-225.

R.M. Scheek, N. Russo, R. Boelens and R. Kaptein, "Sequential Resonance Assignments in DNA 1H NMR Spectra by Two-Dimensional NOE Spectroscopy", J. Am. Chem. Soc., 105, 1983, 2914-2916.


W. Salomons, P. Hofman, R. Boelens and W.G. Mook, "The oxygen isotopic composition of the fraction less than 2 microns (clay fraction) in recent sediments from Western Europe",  Marine Geology 18, (1975) M23 - M28.

Boelens, R. and R. Wever, "Electron-transfer processes in carboxy-cytochrome c oxidase after photodissociation of cytochrome a32+. CO", Biochim. Biophys. Acta  547, 1979, 296-310.

Boelens, R. and R. Wever, "Redox reactions in mixed-valence cytochrome c oxidase", FEBS Letters, 116, 1980, 223-226.

Wilms, J., Dekker, H.L., Boelens, R. and B.F. van Gelder, "The effect of pH and ionic strength on the pre-steady reaction of cytochrome c and cytochrome aa3", Biochim. Biophys. Acta  637, 1981, 168-176.

Boelens, R. Rademaker, H., Pel, R. and R. Wever, "EPR studies of the photodissociation reactions of cytochrome c oxidase-nitric oxide complexes", Biochim. Biophys. Acta 679, 1982, 84-94.

Wever, R., Kast, W.M., Kasinoudin, J. and R. Boelens, "The peroxidation of thiocyanate catalysed by myeloperoxidase and lactoperoxidase", Biochim. Biophys. Acta 709, 1982, 212-219.

Dunford, H.B., Araiso, T., Job, D. Ricard, J., Rutter, R., Hager, L.P., Wever, R., Kast, W.M., Boelens, R., Ellfolk, N. and M. Rönnberg, "Peroxidases" In: The Biological Chemistry of Iron, Donford, H.B., Dolphin, O., Raymond, K. and Sieker, L. (Eds.) Reidel Publishing Co, Dordrecht, 1982, 337-355.

Boelens, R., Wever, R. and B.F. van Gelder,  "Electron transfer after flash photolysis of mixed-valence carboxy-cytochrome c oxidase", Biochim. Biophys. Acta 682, 1982, 264-272.

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Gegenereerd op 2018-09-22 13:10:15

Research Interests

Gene regulation, DNA repair, structure and dynamics of proteins and complexes

Our research focuses on understanding the mechanism of gene regulation, expression and repair. Using NMR spectroscopy we study the structure and dynamics of protein and protein-DNA complexes involved in transcription, translation and DNA repair. Studied examples are the E. coli Lac repressor, bacterial ribosomal initiation factors, the human ERCC1/XPF DNA repair complex and the mechanism of chromatin remodeling. Further studied systems include the photoreceptors PYP and AppA, the Kid/Kis plasmid maintenance system and enzymes, such as subtilisins and lipases.

Specific and non-specific DNA binding by Lac repressor

The lac system is used as a model system to probe in detail structural and dynamic aspects of protein-DNA recognition. Our studies of the complex of Lac headpiece (the DNA binding domain) with different lac operators show the plasticity that both proteins and DNA exhibit in order to optimize interactions. Interaction of DNA-binding proteins with their operators can be preceded by binding to nonspecific DNA. This speeds up the search for the target site by several orders of magnitude. As a model for one-dimensional sliding we determined the solution structure and dynamics of the complex of Lac headpiece with nonspecific DNA.

Kalodimos et al, EMBO J. 21 (2002) 2866-76, Science 305 (2004) 386-9, Chem.Rev. 104 (2004) 3567-86; Romanuka et al, J Mol Biol 390 (2009) 478-8; Loth et al, J BNMR 56 (2013) 41-9


Nucleotide Excision DNA repair

In collaboration with Jan Hoeijmakers (Erasmus MC, Rotterdam) we study the heterodimeric complex of the C-terminal parts of the human Nucleotide Excision DNA repair proteins XPF and ERCC1. The structure explains how ERCC1 targets the endonuclease XPF to the DNA damage site. Subsequent studies of the central domain of ERCC1 accounts for binding of ERCC1/XPF at a ds/ssDNA junction near the DNA lesion.

Tripsianes et al, Structure 13 (2005) 1849-58; Das et al, Proteins 70 (2008) 1551–63, Structure 20 (2012) 667-75


Translation initiation

Bacteria require three initiation factors, IF1, IF2 and IF3, to start protein synthesis. In collaboration with Claudio Gualerzi (Camerino, Italy) we study the structure, function and dynamics of these initiation factors, the changes therein upon interaction with ribosomal subunits, and in GTP and GDP bound states.

Meunier et al, EMBO J 19 (2000) 1918-26; Guennegues et al, EMBO J 19 (2000) 5233-40; Milon et al, PNAS 103 (2006), 13962-7; Wienk et al, JBC 287 (2012), 10922-32


Biomolecular docking

In collaboration with Alexandre Bonvin (Utrecht University) we developed the program HADDOCK for modeling protein-protein complexes that makes use of biochemical and/or biophysical interaction data such as resulting from NMR titration experiments or mutagenesis data. We used it for modeling E2-E3 ubiquitination complexes such as the complex of the human transcription factor CNOT4 and the ubiquitin conjugating enzyme UbcH5B (collaboration with Marc Timmers, UMCU) and the ubiquitination complexes of Rad8 and Rad16 (collaboration with Titia Sixma, NKI, Amsterdam).

Dominguez et al., J Am Chem Soc 125(2003) 1731-37, Structure 12(2004) 633-44; Hibbert et al, PNAS 108 (2011) 5590-5; Huang et al, J Mol Biol 385 (2011), 507-19

Gegenereerd op 2018-09-22 13:10:15

BSc Scheikunde, Struktuuranalyse

MSc MCLS, cMLS, Introduction NMR

MSc MCLS, Molecular Recognition, NMR and protein-DNA recognition

MSc MCLS, Advanced NMR

BSc College Pharmaceutical Sciences, Analyse, Introduction NMR

Bijvoet Summerschool, Biomolecular NMR

EMBO Advanced NMR course

Gegenereerd op 2018-09-22 13:10:15

Lid van verschillende beoordelingscommissies, adviescommissies en editorial boards, bestuurslid van de Nederlandse NMR Discussie Groep en Stichting NMR (Utrecht).

Gegenereerd op 2018-09-22 13:10:15
Volledige naam
prof. dr. R. Boelens Contactgegevens

Nicolaas Bloembergengebouw, kamer 1.15
Padualaan 8, 3584 CH Utrecht

Bereikbaar via Kruytgebouw -> 1e verdieping oost -> loopbrug naar Sjoerd Groenmangebouw

Universiteit Utrecht, NMR
Padualaan 8, 3584 CH Utrecht

Telefoon (secr): +31 30 253 2652

Telefoon (direct): +31 30 253 4035

Gegenereerd op 2018-09-22 13:10:15
Laatst bijgewerkt op 13-06-2018