dr. S.G.D. (Stefan) Rüdiger
Gegenereerd op 2018-09-22 19:04:07


A key challenge in molecular medicine is to develop cures for diseases for which no cure exists – such as Alzheimer, Parkinson or ALS, but also many other diseases with dramatic impact for the affected individual such as ataxias or cystic fibrosis. These diseases have in common that the molecular cause is related to uncontrolled consequences of protein damage and aggregation. Our body is not unprotected against protein damage. The fidelity of protein shape in the cell is maintained by a powerful proteostasis network, in which molecular chaperones and proteases play a key role. This networks supresses the appearance of most folding related diseases for the best part of our life. However, why does it suddently fail when we get older? Why do some individuals get a protein-aggregation related disease and others do not? What is the impact of the proteostasis network for the development of an entire organism? Can we boost the cellular defense system to prevent the origin of the disease, or at least prevent progress of the diseases for some cases? My group aims to understand protein folding processes in the cell and their consequence for the origin of fatal diseases.

Our research is supported by Marie Curie Actions of the EU. Stefan Rüdiger coordinates the FP7 ITN “ManiFold”, the only Innovative Doctoral Programme in the Life Sciences that had been funded in the 2011/2012 call. The Rüdiger group also participates in the FP7 ITN “WntsApp”, coordinated by our long-term collaborator Madelon Maurice, UMC Utrecht. We are supported by the Alzheimer Charity ISAO for the project "Chaperoning Tau aggregation" and by the ZonMW TOP grant "Chaperoning axonal transport in neurodegenrative disease".

Current external research support
NWO - Nederlands Organisation for Scientific Research (PI):
ZonMW TOP Grant "Chaperoning axonal transport in neurodegenerative disease"
ISAO  - Internationale Stichting Alzheimer Onderzoek (Main applicant)
Marie-Curie ITN "WntsApp" (PI)
Marie-Curie ITN-IDP "ManiFold" (Programme Leader and PI)

Previous research support
NWO Graduate Programme (Programme Leader)
NWO BAZIS equipment grant (Project Leader)
NWO VIDI grant (Main applicant)
Marie-Curie Excellence Grant (Main applicant)Utrecht University High Potential Grant (Main applicant, joint grant with Dr Madelon Maurice, UMCU)

Current group members
Tania Morán Luengo (PhD student Marie Curie ITN-IDP ManiFold)
Magdalena Wawrzyniuk (PhD student Marie Curie ITN WntsApp)
Luca Ferrari (PhD student Marie Curie ITN WntsApp)
Margreet Koopman (PhD student ZonMW TOP Chaperoning Axonal Transport)
Fatih Boogard (MSc student Molecular & Cellular Life Sciences)
Gerarda van der Kamp (MSc student Molecular & Cellular Life Sciences)
Sem Halters (MSc student Molecular & Cellular Life Sciences)
Douwe den Bulte (BSc student Molecular Life Sciences)
Toveann Ahinäs (Erasmus student)


Strategic themes / Focus areas
Involved in the following study programme(s)
Scientific expertise
Alzheimer Disease
protein folding
Molecular chaperones
Protein aggregation
Wnt signalling
Intrinsically disordered proteins
Scaffold proteins
Protein damage
Molecular Life Sciences
Cancer mutations
Peptide arrays

The Rüdiger group (2018)

The Rüdiger group (2017)

A chaperone relay team to prepare proteins to fold on their own

Cover Molecular Cell (2018)
Gegenereerd op 2018-09-22 19:04:07
Curriculum vitae

Stefan Rüdiger graduated in Chemistry at Heidelberg University (1995) and obtained the PhD from Freiburg University (2000, summa cum laude). After a postdoc with Sir Alan Fersht (Cambridge University and Medical Research Council, supported by Long Term Fellowships of EMBO and the Marie-Curie Programme) he started his own group in Utrecht in 2004. He has the ius promovendi of Utrecht University.

His work centres on the molecular mechanisms or protein folding and chaperoning in the cell. A particular focus is on understanding the mechanism of chaperone machines. Recent work provided a mechanism of action for the key chaperone systems Hsp70 and Hsp90. The Rüdiger group now focusses to understand how these chaperones control protein aggregation in neurodegenerative diseases, such as Alzheimer, Parkinson and Huntington. A key finding of his group decribed a structural model of the Hsp90 chaperone in complex with the Alzheimer protein Tau. His group also studies how tumour mutations effect protein stability of signalling molecules, using the Wnt signalling cascade as model, in collaboration with the group of Madelon Maurice at the UMCU.

He is coordinator of the bachelor courses Biomolecular Chemistry and Protein Folding and Assembly and of the master course Concepts in Molecular Life Sciences. He is also involved in the master course “Molecules and Cells”.

Rüdiger is Marie Curie Excellence Team Leader (2005), VIDI (2005) and High Potential of Utrecht University (2006). He is Coordinator of the Marie-Curie ITN Innovatove Doctoral Programme "ManiFold" (2012), tracker of the NWO Graduate Programme of the Bijvoet School (2012) and he was Director of the Utrecht Summer School "Exploring Nature's Molecular Machines" (2012-2016). 

Gegenereerd op 2018-09-22 19:04:07

Google Scholar profile:

International publications
Publications until 2009 are published as S. Rüdiger, since 2010 including the middle initials as S.G.D Rüdiger.

50 Radli M, Rüdiger SGD#.
Dancing with the diva: Hsp90-client interactions
J Mol Biol. 2018; in the press. (# = corresponding author)
igh resolution cover:

49 Morán Luengo T, Kityk R, Mayer MP#, Rüdiger SGD#.
Hsp90 breaks the deadlock of the Hsp70 chaperone system.
Mol Cell. 2018;70:545-552 (cover story). (# = corresponding author)
link for free download, valid for first 50 days:

48 Radli M, Rüdiger SGD#.
Picky Hsp90 - every game with a different mate.
Mol Cell. 2017;67:899-900 (invited preview). (# = corresponding author)

47 Radli M, Veprintsev DB, Rüdiger SGD#.
Production and purification of human Hsp90β in Escherichia coli.
PLoS One. 2017;12(6):e0180047. doi:10.1371/journal.pone.0180047. (# = corresponding author)

46 Anvarian Z, Nojima H, van Kappel EC, Madl T, Spit M, Viertler M, Jordens I, Low TY, van Scherpenzeel R, Kuper I, Richter K, Heck AJR, Boelens R, Vincent JP, Rüdiger SGD#, Maurice MM#. Axin cancer mutants form nano-aggregates to rewire the Wnt signaling network.
Nature Struct Mol Biol. 2016;23:324-32. (# = corresponding author)

45 Hagemans D, van Belzen IAEM, Morán Luengo T, Rüdiger SGD#.
A script to highlight hydrophobicity and charge on protein surfaces.
Frontiers Mol Biosci 2015;2:56. (# = corresponding author)

44 Sinnige T, Karagöz GE, Rüdiger SGD#.
Protein Folding and Chaperones.
Encyclopedia of Life Sciences (ELS). John Wiley & Sons, Ltd: Chichester (2015). (# = corresponding author)

43 Karagöz GE, Rüdiger SGD#.
Hsp90 interaction with clients.
Trends Biol Sci. 2015;40:117-125. (# = corresponding author)

42 Karagöz GE, Duarte AMS, Akoury E, Ippel H, Biernat J, Morán Luengo T, Radli M, Didenko T, Nordhues BA, Veprintsev DB, Dickey CA, Mandelkow E, Zweckstetter M, Boelens R, Madl T#, Rüdiger SGD#.
Hsp90-Tau complex reveals molecular basis for specificity in chaperone action.
Cell. 2014;156:963-974. (# = corresponding author)

41 Minde DP, Radli M, Forneris F, Maurice MM#, Rüdiger SGD#. Large extent of disorder in Adenomatous Polyposis Coli offers a strategy to guard Wnt signalling  against point mutations. 
PLoS One. 2013;8:e77257. (# = corresponding author)

40 Xue B, Romero PR, Noutsou M, Maurice MM, Rüdiger SGD, William AM Jr, Mizianty MJ, Kurgan L, Uversky VN, Dunker AK.
Stochastic machines as a colocalization mechanism for scaffold protein function.
FEBS Lett. 2013;587:1587-91.  

39 Minde DP, Maurice MM#, Rüdiger SGD#.
Determining biophysical protein stability in lysates by a fast proteolysis assay, FASTpp.
PLoS One. 2012;7:e46147. (# = corresponding author)

38 Suijkerbuijk SJ, van Dam TJ, Karagöz GE, von Castelmur E, Hubner NC, Duarte AMS, Vleugel M, Perrakis A, Rüdiger SGD, Snel B, Kops GJ.
The vertebrate mitotic checkpoint protein BUBR1 is an unusual pseudokinase.
Dev Cell. 2012;22:1321-9.  

37 Li Y, Karagöz GE, Seo YH, Zhang T, Jiang Y, Yu Y, Duarte AMS, Schwartz SJ, Boelens R, Carroll K#, Rüdiger SGD#, Sun D#.
Sulforaphane inhibits pancreatic cancer  through disrupting Hsp90-p50(Cdc37) complex and direct interactions with amino acids residues of Hsp90.
J Nutr Biochem. 2012;23:1617-26. (# = corresponding author)

36 Tauriello DV, Jordens I, Kirchner K, Slootstra JW, Kruitwagen T, Bouwman BA, Noutsou M, Rüdiger SGD, Schwamborn K, Schambony A, Maurice MM.
Wnt/β-catenin signaling requires interaction of the Dishevelled DEP domain and C terminus with  a discontinuous motif in Frizzled.
Proc Natl Acad Sci U S A. 2012;109:E812-20.  

35 Didenko T, Duarte AM, Karagöz GE, Rüdiger SGD#.
Hsp90 structure and function studied by NMR spectroscopy.
Biochim Biophys Acta. 2012;1823:636-47. (# = corresponding author)

34 Minde DP, Anvarian Z, Rüdiger SGD#, Maurice MM#.
Messing up disorder: how do missense mutations in the tumor suppressor protein APC lead to cancer?
Mol Cancer. 2011;10:101. (# = corresponding author)

33 Karagöz GE, Sinnige T, Hsieh O, Rüdiger SGD#.
Expressed protein ligation for a large dimeric protein.
Protein Eng Des Sel. 2011;24:495-501. (# = corresponding author)

32 Katz C, Levy-Beladev L, Rotem-Bamberger S, Rito T, Rüdiger SGD, Friedler A.
Studying protein-protein interactions using peptide arrays.
Chem Soc Rev. 2011;40:2131-45.  

31 Karagöz GE, Duarte AMS, Ippel H, Uetrecht C, Sinnige T, van Rosmalen M, Hausmann J, Heck AJR, Boelens R, Rüdiger SGD#.
N-terminal domain of human Hsp90 triggers binding to the cochaperone p23.
Proc Natl Acad Sci U S A. 2011;108:580-5. (# = corresponding author)

30 Noutsou M, Duarte AMS, Anvarian Z, Didenko T, Minde DP, Kuper I, de Ridder I,  Oikonomou C, Friedler A, Boelens R, Rüdiger SGD#, Maurice MM#.
Critical scaffolding  regions of the tumor suppressor Axin1 are natively unfolded.
J Mol Biol. 2011;405:773-86. (# = corresponding author)

29 Didenko T, Boelens R, Rüdiger SGD#.
3D DOSY-TROSY to determine the translational diffusion coefficient of large protein complexes.
Protein Eng Des Sel. 2011;24:99-103. (# = corresponding author)

28 Sinnige T, Karagöz GE, Rüdiger SGD#.
Protein Folding and Chaperones.
Encyclopedia of Life Sciences (ELS). John Wiley & Sons, Ltd: Chichester (2010). (# = corresponding author)

27 Tsaytler PA, Krijgsveld J, Goerdayal SS, Rüdiger S, Egmond MR.
Novel Hsp90 partners discovered using complementary proteomic approaches.
Cell Stress Chaperones. 2009;14:629-38.  

26 Rotem S, Katz C, Benyamini H, Lebendiker M, Veprintsev D, Rüdiger S, Danieli T, Friedler A.
The structure and interactions of the proline-rich domain of ASPP2.
J Biol Chem. 2008;283:18990-9.  

25 Katz C, Benyamini H, Rotem S, Lebendiker M, Danieli T, Iosub A, Refaely H, Dines M, Bronner V, Bravman T, Shalev DE, Rüdiger S, Friedler A.
Molecular basis  of the interaction between the antiapoptotic Bcl-2 family proteins and the proapoptotic protein ASPP2.
Proc Natl Acad Sci U S A. 2008;105:12277-82.  

24 Rodriguez F, Arséne-Ploetze F, Rist W, Rüdiger S, Schneider-Mergener J, Mayer  MP, Bukau B. Molecular basis for regulation of the heat shock transcription factor sigma32 by the DnaK and DnaJ chaperones.
Mol Cell. 2008;32:347-58.  

23 Mayer S, Rüdiger S, Ang HC, Joerger AC, Fersht AR.
Correlation of levels of folded recombinant p53 in escherichia coli with thermodynamic stability in vitro.
J Mol Biol. 2007;372:268-76.   

22 Vega CA, Kurt N, Chen Z, Rüdiger S, Cavagnero S.
Binding specificity of an alpha-helical protein sequence to a full-length Hsp70 chaperone and its minimal substrate-binding domain.
Biochemistry. 2006;45:13835-46.  

21 Yu GW, Rüdiger S, Veprintsev D, Freund S, Fernandez-Fernandez MR, Fersht AR.
The central region of HDM2 provides a second binding site for p53.
Proc Natl Acad Sci U S A. 2006;103:1227-32.   

20 Friedler A, DeDecker BS, Freund SMV, Blair C, Rüdiger S, Fersht AR.
Structural  distortion of p53 by the mutation R249S and its rescue by a designed peptide: implications for "mutant conformation".
J Mol Biol. 2004;336:187-96.  

19 Vandenbroeck K, Alloza I, Brehmer D, Billiau A, Proost P, McFerran N, Rüdiger S, Walker B.
The conserved helix C region in the superfamily of interferon-gamma  /interleukin-10-related cytokines corresponds to a high-affinity binding site for the HSP70 chaperone DnaK.
J Biol Chem. 2002;277:25668-76.   

18 Rüdiger S, Freund SMV, Veprintsev DB, Fersht AR.
CRINEPT-TROSY NMR reveals p53  core domain bound in an unfolded form to the chaperone Hsp90.
Proc Natl Acad Sci  U S A
. 2002;99:11085-90.   

17 Hansson LO, Friedler A, Freund S, Rüdiger S, Fersht AR.
Two sequence motifs from HIF-1alpha bind to the DNA-binding site of p53.
Proc Natl Acad Sci U S A. 2002;99:10305-9.   

16 Friedler A, Hansson LO, Veprintsev DB, Freund SMV, Rippin TM, Nikolova PV, Proctor MR, Rüdiger S, Fersht AR.
A peptide that binds and stabilizes p53 core domain: chaperone strategy for rescue of oncogenic mutants.
Proc Natl Acad Sci U  S A. 2002;99:937-42.   

15 Patzelt H, Rüdiger S, Brehmer D, Kramer G, Vorderwülbecke S, Schaffitzel E, Waitz A, Hesterkamp T, Dong L, Schneider-Mergener J, Bukau B, Deuerling E.
Binding specificity of Escherichia coli trigger factor.
Proc Natl Acad Sci U S A. 2001;98:14244-9.   

14 Schaffitzel E, Rüdiger S, Bukau B, Deuerling E.
Functional dissection of trigger factor and DnaK: interactions with nascent polypeptides and thermally denatured proteins.
Biol Chem. 2001;382:1235-43.  

13 Brehmer D, Rüdiger S, Gässler CS, Klostermeier D, Packschies L, Reinstein J, Mayer MP, Bukau B. Tuning of chaperone activity of Hsp70 proteins by modulation of nucleotide exchange.
Nature Struct Biol. 2001;8:427-32.  

12 Rüdiger S, Schneider-Mergener J, Bukau B.
Its substrate specificity characterizes the DnaJ co-chaperone as a scanning factor for the DnaK chaperone. 
EMBO J. 2001;20:1042-50.  

11 Rüdiger S, Mayer MP, Schneider-Mergener J, Bukau B.
Modulation of substrate specificity of the DnaK chaperone by alteration of a hydrophobic arch.
J Mol Biol. 2000;304:245-51.  

10 Mayer MP, Rüdiger S, Bukau B.
Molecular basis for interactions of the DnaK chaperone with substrates.
Biol Chem. 2000;381:877-85.  

9 Mayer MP, Schröder H, Rüdiger S, Paal K, Laufen T, Bukau B.
Multistep mechanism of substrate binding determines chaperone activity of Hsp70.
Nature Struct Biol. 2000;7:586-93.  

8 Mogk A, Tomoyasu T, Goloubinoff P, Rüdiger S, Röder D, Langen H, Bukau B.
Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpB.
EMBO J. 1999;18:6934-49.  

7 Knoblauch NT, Rüdiger S, Schönfeld HJ, Driessen AJ, Schneider-Mergener J, Bukau B.
Substrate specificity of the SecB chaperone.
J Biol Chem. 1999;274:34219-25.  

6 Brix J, Rüdiger S, Bukau B, Schneider-Mergener J, Pfanner N.
Distribution of  binding sequences for the mitochondrial import receptors Tom20, Tom22, and Tom70  in a presequence-carrying preprotein and a non-cleavable preprotein.
J Biol Chem. 1999;274:16522-30.  

5 Rüdiger S, Buchberger A, Bukau B.
Interaction of Hsp70 chaperones with substrates.
Nature Struct Biol. 1997;4:342-9.  

4 Rüdiger S, Germeroth L, Schneider-Mergener J, Bukau B.
Substrate specificity  of the DnaK chaperone determined by screening cellulose-bound peptide libraries. 
EMBO J. 1997;16:1501-7.  

3 McCarty JS, Rüdiger S, Schönfeld HJ, Schneider-Mergener J, Nakahigashi K, Yura T, Bukau B. Regulatory region C of the E. coli heat shock transcription factor, sigma32, constitutes a DnaK binding site and is conserved among eubacteria.
J Mol Biol. 1996;256:829-37.  

2 Gamer J, Multhaup G, Tomoyasu T, McCarty JS, Rüdiger S, Schönfeld HJ, Schirra C, Bujard H, Bukau B.
A cycle of binding and release of the DnaK, DnaJ and GrpE chaperones regulates activity of the Escherichia coli heat shock transcription factor sigma32.
EMBO J. 1996;15:607-17.  

1 Herdegen T, Rüdiger S, Mayer B, Bravo R, Zimmermann M.
Expression of nitric oxide synthase and colocalisation with Jun, Fos and Krox transcription factors in spinal cord neurons following noxious stimulation of the rat hindpaw.
Brain Res Mol Brain Res. 1994;22:245-58.  



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Gegenereerd op 2018-09-22 19:04:07


A key challenge in molecular medicine is to develop cures for diseases for which no cure exists – such as Alzheimer, Parkinson or ALS, but also many other diseases with dramatic impact for the affected individual such as ataxias or cystic fibrosis. These diseases have in common that the molecular cause is related to uncontrolled consequences of protein damage and aggregation. Our body is not unprotected against protein damage. The fidelity of protein shape in the cell is maintained by a powerful proteostasis network, in which molecular chaperones and proteases play a key role. This networks supresses the appearance of most folding related diseases for the best part of our life. However, why does it suddently fail when we get older? Why do some individuals get a protein-aggregation related disease and others do not? Can we boost the cellular defense system to prevent the origin of the disease, or at least prevent progress of the diseases for some cases? My group aims to understand protein folding processes in the cell and their consequence for the origin of fatal diseases. We connect three related research themes:

The cell controls shaping of newly-made proteins and the removal of damaged or problematic proteins. This control is essential for life, derailing of this control is fatal. The most prominent failure is the aggregation of the protein Tau, which ultimately leads to Alzheimer Disease. Resetting control of Tau maintenance would provide a causal therapy for Alzheimer, but at present this fails due to a lack of understanding at molecular level. Molecular chaperones such as the Hsp90 chaperone are the first line of the cellular defense system against protein damage and aggregation. The chaperones are part of the proteostasis network, the natural defense system against protein damage problems. Hsp90 interacts in vivo and in vitro with the Tau protein. We have recently described a structural model of an Hsp90-Tau complex, showing the Tau protein behaves as a bona fide client of the Hsp90 chaperone. We found Hsp90 to bind to the Tau’s microtubule-binding repeat region, which forms the toxic aggregates. Together this suggests a direct role for Hsp90 in dealing with Tau aggregation. We hypothesize that molecular chaperones typically counter aggregation of Tau, but a decrease in chaperoning capacity at higher age may allow fatal aggregation to proceed. Our aim is now to test the function of the natural defense system in the origin of of Alzheimer Disease. We rare currently exploring whether and how molecular chaperones can control aggregation and disaggregation of Alzheimer fibrils.

Signalling proteins are key clients of the chaperone Hsp90, many of which are membrane-standing signalling proteins. We work on understanding the link between protein quality control and cancer. We analyse the mechanism of action of cancer point mutants in tumour suppressors, using the Wnt signalling cascade as a model. We investigate how cancer point mutations in a key scaffold protein induced tumour growth. In particular, we analyse the hypothesis that mutations may lead to structural destabilisation and subsequent oligomerisation of tumour suppressor proteins. This is important as such changes may affect lead to loss of interaction with crucial binding partners, but it may also form novel, abberrant and potentially toxic interactions. A key aim for us is to understand the interaction of the natural defense against protein damage, the proteostasis network, with nanoaggregates.

Hsp70 chaperones act early and Hsp90 late in the folding path, yet the molecular basis of this timing had been enigmatic. We obtained a structural model of Hsp90 in complex with its natural substrate, the intrinsically disordered Tau protein. Our model resolved the paradox on how Hsp90 specifically selects for late folding intermediates but also for some intrinsically disordered proteins – through the eyes of Hsp90 they look the same. It is striking, however, that key details of the active cycle of Hsp90 are known, but the big picture is still enigmatic - what is the actual function of Hsp90 chaperones in the cell? Our work is dedicated to provide an answer to this question. We recenty indentified the molecular mechanism why and how the Hsp70 and Hsp90 form a partnership to fold proteins.


The trademark of our work is answering burning biological questions with an interdiciplinary range of methods, to make use of the wealth of methods offered on the Utrecht campus, from molecule to organism.

We have expertise to prepare complex proteins for biological studies. We characterise them using biochemical assays, such as folding assays or fluorescence methods to analyse protein stability and protein-protein interactions. We use integrated structural biology approaches e.g by combining NMR spectroscopy and SAXS to characterise protein complexes or EM methods to get structural insights into biological processes. We are currently transferring insights obtained by our structural and biochemical studies into living cells.


Stefan Rüdiger’s recent  activities include:

Chair of the Marie-Curie Innovative Doctoral Programme "ManiFold", an international, interdisciplinary project within the Bijvoet Graduate School at Utrecht University with 11 EU funded PhD student positions:

PI and Work package leader in the Marie-Curie ITN WntsApp, an interational interdisciplinary project focussing on the Wnt signalling cascade:

Coordinator of the NWO-funded Bijvoet Graduate Programme, that offers 4 PhD student positions within the school:

Director of the Utrecht Summer School “Exploring Nature’s Molecular Machines” 2012-2016. For more information and applications:

Coordinator of the NWO-funded equipment grant BAZIS at the Bijvoet Center.


The ManiFold project is covered in an official Horizon2020 video:





Gegenereerd op 2018-09-22 19:04:07

Stefan Rüdiger acquired teaching experience in a braod range of different forms on teaching, covering a broad range of subjects in structural biology and biochemistry. He participates or had been involved in the following teaching activities:

1. Teaching organisation

1.1 Initiative to develop a new bachelor curtriculum in Molecular Life Sciences (2012-2014)
Drafting of a new interdisciplinary curriculum on the edge of chemistry, biology and pharmacy. Main goals had been to improve number and quality of the students entering the master programme Molecular and Cellular Life Sciences and increasing the number of students in (bio-)chemistry. This started as bottom up initiative and successively gained support within the participating Departments and the Faculty, so that this could start finally in Sep 2014 with 55 students.

1.2 Director Utrecht Summer School Exploring Nature’s Molecular Machines (since 2012)
Coordination, programme assembly and management, selection of candidates, setup of scholarship programme.

1.3 Programme leader NWO Graduate Programme at the Bijvoet Center (since 2013)
Design of the programme and raising funding, lead of implementation and chair of selection committee.

1.4 Programme leader Innovative Doctoral Programme “ManiFold” at the Bijvoet Center (since 2012)
Design of the programme and raising funding, lead of implementation and management, coordination contacts to EU.

1.5 Development new teaching line biochemistry in bachelor chemistry (2007-2008)
Based on these recommendation the course programme in all three bachelor years had been adapted in all three years.

1.6 Chair of the Educational Advisory Committee (OAC) of the Chemistry Department of Utrecht University (since 2016; member since 2010)

1.7 Member committee development new bachelor Science for Life (since 2017)


2. Teaching at Bachelor level

2.1 Bachelor theses for Chemistry students (since 2007; 15 EC)
Supervision of final year bachelor thesis in my research group.

2.2 3rd year bachelor course “Structural Biology” (2005-2010; 15 EC)
Coordination, lectures (6 h), practicum in research lab, research proposal; interdisciplinary course of Biology and Chemistry for students of chemistry, biology and biomedical sciences.

2.3 3rd year bachelor course “Molecular Machines” (2011-now; 7.5 EC)
Course coordination; chemistry students.

2.4 3rd year bachelor course “Molecular Processes” (2011-now; 7,5 EC)
Course coordination, lectures (6 h), practicum in research lab, research proposal, symposion; chemistry students.

2.5 3rd year bachelor course “Research in Molecular Life Sciences” (since 2011, 7.5 EC)
Development of new course, course coordination, lectures, practicum in research lab, research proposal; chemistry students.

2.6 2nd year “Research project” (Since 2007; 7.5 EC)
Supervision of research project of typically 4 students in my research group, final presentation.

2.7 Honoursprogramme chemistry, 2nd year module on protein folding (since 2010)
Development of new module, lectures (3 h), computerpracticum, journal club.

2.8 2nd year Biophysics (2011-2012; 7.5 EC)
Lectures (4 h), practicum in research lab, report.

2.9 2nd year seminar on membrane chemistry (2007, 7.5 EC)
Seminar for students biomedical sciences, presentation.

2.10 1st year short internship (since 2006; 4.5 EC)
Supervision of a student couple in my research group, poster presentation.

2.11 1st year “Chemistry of the Cell” (2009-1014; 7.5 EC)
Development new practicum on basic protein chemistry (cell cracking, purification, spectroscopic characterisation, unfolding and refolding, final report), guest lecture.

2.12 1st year “Biomolecular Chemistry” (2015; 7.5 EC)
Development of entirely new course at the end of the 1st year for all Chemistry and Molecular Life Science students, including practicum; vision is to teach a protein-centered course based on Kuriyan et al. “Molecules of Life”; lectures (16 h), practice groups, practicum.

2.13 Tutor bachelor Chemistry (Since 2005)

2.14 Tutor bachelor Molecular Life Sciences (Since 2014)

3. Teaching at Master level

3.1 Utrecht Summer School “Exploring Nature’s Molecular Machines” (since 2010)
lectures, practicum in research lab, career development workshop.

3.2 Master course “Molecular recognition” (since 2006; 3 EC)
lecture, research symposion and literature seminar

3.3 Supervision of master interships (6 and 9 months; since 2005)

3.4 Supervision of master literature thesis (7.5 EC/5 weeks; since 2004)

3.5 Master Class “Advanced strategies in protein science” (2008-2012, 3 EC)
Development of new practical course and carreer workshop.

3.6 Master course “Research in Molecular Life Sciences” (since 2011, 7.5 EC)
Development of new course, course coordination, lectures (2 h), practicum in research lab, research proposal; chemistry students.

4. Teaching at graduate student level

4.1 Weekly research seminar and journal club with my own group (since 2005)

4.2 Setting up interdisciplinary monthly journal group “Science at lunch” with biochemistry and cell biology groups (2008-2010)

4.3 PhD examinations
at Utrecht University, Wageningen University, Nijmegen University and Florence University

4.4 Introductory course for IB Graduate School (since 2007; 3 EC)

5. Outreach at high school level

5.1 Practicum “Preventing Speed Dating”
Setting up of a practicum on protein folding for High Schools as part of the “Rector’s league of Utrecht University (7x since 2006 on schools (coverage by Algemeen Dagblad in 2006), now regularly in our research lab).

5.2 Lecture at “Beta-Festval” at high school Broklede (2011-2012)
Lecture on Roger Kornberg’s Nobel Prize on RNA polymerase, targeted at 5/6 VWO students (last two years of High School).

5.3 project school link (2011-2014)
Supervision of a project with a school teacher to develop experiments and material for biochemistry teaching at schools.

5.4 Laboratory tours
High school students and elementary school children

6. Teaching activities as PhD student and postdoc

6.1 Journal club at Cambridge Centre for Protein Engineering (2001-2004)
Introduced on my initiative and organised by myself.

6.2 Introductory seminar biochemistry (1997-1999)
weekly seminar for 1st year/2nd semester medicine students at Freiburg University

6.3 Biochemistry practicum (1997-1999)
Biochemistry practicum for medicine and detistry students at Freiburg University.

6.4 Advanced practical course on mechanisms of the control of transcription and the folding of proteins (1996)
Practical course at ZMBH Heidelberg for advanced Biology students (3rd/4th year), organised by the Bujard and Bukau groups.


For each course the year of contribution is indicated, so are the total EC value for the student.

Gegenereerd op 2018-09-22 19:04:07
Additional functions and activities

* Coordinator Marie-Curie ITN-IDP Manifold
* Vice-Chair H2020 MCSA review panel for ITNs
* Member of Marie-Curie FP7 and H2020 evaluation panels
* Member of NWO VENI grant panel
* Peer reviewer for (inter-)national funding organisations and charities
* Editorial Board Member for "Scientific Reports"
* Reviewing Editor for "Frontiers"
* Peer reviewer for international scientific journals
* Director Summer School "Exploring Nature's Molecular Machines"
* Chair of the Educational Advisory Commitee (OAC) of the Chemistry Department
* Chair of the Faculty Library Committee of the Faculty of Sciences
* Chair of the advisory board of the Paulusschool in Utrecht
* Sailing instructor at Cam Sailing Club, Cambridgeshire

Gegenereerd op 2018-09-22 19:04:07
Full name
dr. S.G.D. Rüdiger Contact details
Hugo R. Kruytgebouw

Padualaan 8
Room O 704
The Netherlands

Phone number (direct) +31 30 253 3394
Phone number (department) +31 30 253 2184
Gegenereerd op 2018-09-22 19:04:08
Last updated 12.09.2018