Geerten W Vuister

Personal Details

Geerten W. Vuister
Geerten Vuister headshot Department: Molecular and Cell Biology
0116 229 7076
Lancaster Rd, LE1 7HB
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Prof. Geerten W. Vuister studied physical chemistry and computational science at the University of Groningen, The Netherlands. Under the supervision of Profs Boelens and Kaptein he obtained his Ph.D. cum laude at Utrecht University in 1991. Subsequently, he became a visiting fellow at the National Institutes of Health (Bethesda, USA) working in the NMR group of Dr. A. Bax. In 1994 he received a KNAW (Royal Dutch Academy of Sciences) young investigator award and was appointed assistant professor (Utrecht University), followed by an appointments as associate professor (Radboud University Nijmegen) and professor in Protein Biophysics in 2008 (Radboud University Nijmegen). In 2010, he moved to the University of Leicester and now holds a chair in Structural Biology

Prof. Vuister is the chair of the Collaborative Computational Project for NMR (CCPN, He also serves as a member of the international wwPDB NMR validation taskforce ( and chairs the NMR exchange format (NEF) development group (


  • 1984 Bachelor of Science, University of Groningen, The Netherlands.
  • 1987 Master of Science, University of Groningen, The Netherlands.
  • 1991 PhD. cum laude, Utrecht University, The Netherlands.
  • 1997 University Teaching Qualification, Utrecht, The Netherlands


Prof. Vuister has great enthusiasm for all teaching related to biomolecular structure and functioning, in particular related to ion channel regulation, NMR techniques and methods, structure calculation and validation, and data remediation and management. He has been a regular contributor to various national and international PhD and summerschools in the area of NMR (BNRA/Bijvoet, HWB-NMR, EMBO).


  1. Bate, N., Caves, R., Skinner, S.P., Goult, B.T., Basran, J., Mitcheson, J.S. & Vuister, G.W. (2018)A Novel Mechanism for Calmodulin Dependent Inactivation of Transient Receptor Potential Vanilloid 6”, Biochemistry, in press.
  2. Skinner, S. P., Fogh, R. H., Boucher, W., Ragan, T. J., Mureddu, L. G., & Vuister, G. W. (2016). CcpNmr AnalysisAssign: a flexible platform for integrated NMR analysis.
  3. Rosato, A., Vranken, W., Fogh, R.H., Ragan, T.J., Tejero, R., Pederson, K., Lee, H-W., Prestegard, J.H., Yee, A., Wu, B., Lemak, A., Houliston, S., Arrowsmith, C.H., Acton, T.B., Xiao, R., Liu, G., Montelione, G.T. & Vuister, G.W. (2015) “The Second Round of Critical Assessment of Automated Structure Determination of Proteins by NMR: CASD-NMR-2013”, J. Biomol. NMR 62, 413-424.
  4. Ragan, T.J., Fogh, R.H., Tejero, R., Vranken, W., Montelione, A., Rosato, A. & Vuister, G.W. (2015) “Analysis of the Structural Quality of the CASD-NMR 2013 Entries” J. Biomol. NMR 62, 527-540.
  5. Gutmanas, A., Adams, P.D., Bardiaux, B., Berman, H.M., Case, D., Fogh, R.H., Guentert, P., Hendrickx, P.M.S., Herrmann, T., Kleywegt, G., Kobayashi, N., Lange, O.F., Markley, J.K, Montelione, G.T., Nilges, M., Ragan, T.J., Schwieters, C.D., Tejero, R., Ulrich, E., Velankar, S., Vranken, W.F., Wedell, J., Westbrook, J., Wishart, D.S. & Vuister, G.W. (2015) “NMR Exchange Format: a unified and open standard for representation of NMR restraint data” Nat. Struct. Mol. Biol 22, 433-34.
  6. Skinner, S.P., Goult, B.T., Fogh, R.H., Boucher, W., Stevens, T.J.S., Laue, E.D. & Vuister, G.W. (2015) “Structure calculation, refinement and validation using CcpNmr Analysis”, Acta Cryst. D71, 154-61.
  7. Lodwick, D., Rainbow, R.D., Rubaiy, H.N., Johi, Al, M., Vuister, G.W., & Norman, R.I. (2014). Sulfonylurea receptors regulate the channel pore in ATP-sensitive potassium channels via an intersubunit salt bridge. Biochem J. 464, 343–354.
  8. Vranken, W.F., Vuister, G.W. & Bonvin, A.M.J.J. (2015) 
"NMR-based modeling and refinement of protein 3D structures."
 Methods Mol. Biol. 1215, 351-80.
  9. Montelione, G. T., Nilges, N., Bax, A., Guentert, P. Herrmann, T., Richarson, J.S., Schwieters, C.D., Vranken, W.F., Vuister, G.W., Wishart, D.S., Berman, H.M., Kleywegt, G.J., Markley, J.L (2013) “Recommendations of the wwPDB NMR Validation Task Force.”, Structure 21, 1563–1570
  10. Ronchieri, E., Verlato, M., Salomoni, D., Dalla Torre, G., Italiano, A., Ciaschini, V., Andreotti, D., Dal Pra, S., Touw, W.G., Vriend, G. & Vuister, G.W. (2013) “Accessing Scientific Applications through the WNoDeS Cloud Virtualization Framework” Proceedings of Science (PoS) 11/2013; 029, eISSN:1824-8039.
  11. Vuister, G.W., Fogh, R.H., Hendrickx, P.M.S., Doreleijers, J.F.D. & Gutmanas, A. (2013) "An overview of tools for the validation of biomacromolecular NMR structures", J. Biomol. NMR 58, 259-85
  12. Kovalevskaya, N., van der Waterbeemd, M. van der, Bokhovchuk, F.M., Bate, N. Bindels, R.J.M., Hoenderop, J.G.J & Vuister, G.W. (2013) "Structural analysis of calmodulin binding to ion channels demonstrates the role of its plasticity in regulation", Pflugers Arch – Eur. J.Physiol. 465, 1507-19
  13. Cilia, E., Vuister, G.W. & Lennaerts, T. (2012) “Accurate prediction of the dynamical changes within the second PDZ domain of PTP1e”, PLOS Comp.Biol. 8, e1002794
  14. Wassenaar, T.A., van Dijk, M., Loureiro-Ferreira, N., van der Schot, G., de Vries, S.J., Schmitz, C., van der Zwan, J., Boelens, R., Giachetti, A., Ferella, L., Rosato, A., Bertini, I., Herrmann, T., Jonker, H.R.A., Bagaria, A., Jaravine, V., Güntert, P., Schwalbe, H., Vranken, W.F., Doreleijers, J.F., Vriend, G., Vuister, G.W., Franke, D., Kikhney, A., Svergun, D.I., Fogh, R., Ionides, J., Laue, E.D., Spronk, C.A.E., Verlato, A., Badoer, S., Dal Pra, S., Mazzucato, M., Frizziero, E. & Bonvin, A.M.J.J. (2012) “WeNMR: Structural Biology on the Grid”, J. Grid Comp. 10, 743-67.
  15. Doreleijers, J.F., Sousa da Silva, A.W., Krieger, E., Nabuurs, S.B, Spronk, C.A.E.M., Stevens, T.S., Vranken. W.F., Vriend, G. & Vuister, G.W. (2012) “CING; an integrated residue-based structure validation program suite “, J. Biomol. NMR 54, 267-83.
  16. Breukels, V., Touw, W.G., & Vuister, G.W. (2012). “Structural and dynamical aspects of Ca2+ and Mg2+ binding of the regulatory domains of the sodium-calcium exchanger.” J. Biomol. NMR 54, 115-21.
  17. Grahl, S. Maillard, J., Spronk, C.A.E., Vuister, G.W. & Sargent, F. (2012) “Overlapping transport and chaperone-binding functions within a bacterial twin-arginine signal peptide.”, Mol. Microbiol. 83, 1254-67.
  18. Rosato, A., Aramini, J.M., Arrowsmith, C., Bagaria, A., Baker, D., Cavalli, A., Doreleijers, J.F., Eletsky, A., Giachetti, A., Guerry, P., Gutmanas, A., Güntert, P., He, Y., Herrmann, T., Huang, Y.J., Jaravine, V., Jonker, H.R.A., Kennedy, M.A., Lange, O.F., Liu, G., Malliavin, T.E., Mani, R., Mao, B., Montelione, G.T., Nilges, M., Rossi, P., van der Schot, G., Schwalbe, H., Szyperski, T.A., Vendruscolo, M., Vernon, R., Vranken, W.F., de Vries, S., Vuister, G.W., Wu, B., Yang, Y. & Bonvin, A.M.J.J. (2012) “Blind testing of routine, fully automated determination of protein structures from NMR data”, Structure 20, 227-236.
  19. Breukels, V., Touw, W.G., & Vuister, G.W. (2012). “Structural and dynamical aspects of Ca2+ and Mg2+ binding of the regulatory domains of the sodium-calcium exchanger.” Biochem Soc. Trans. 40, 409-414.
  20. Doreleijers, J. F., Vranken, W. F., Schulte, C., Markley, J. L., Ulrich, E. L., Vriend, G., & Vuister, G. W. (2012) “NRG-CING: integrated validation reports of remediated experimental biomolecular NMR data and coordinates in wwPDB.” Nucl. Acids Res. 40, D519–D524.
  21. Kovalevskaya, N.Z., Bokhovchuk, F.M. & Vuister, G.W. (2011) “The TRPV5/6 calcium channels contain multiple calmodulin binding sites with differential binding properties”, J. Struct. Func. Genomics 80, 28-33.
  22. Breukels, V., Konijenberg, A., Nabuurs, S.M., Touw, W.G. & Vuister, G.W. (2011) “The second Ca2+ binding domain of the sodium-calcium exchanger is predominantly loaded with one Mg2+ ion under physiological conditions.” Biochemistry 50, 8804-12.
  23. Kovalevskaya, N.Z., Schilderink, N. & Vuister, G.W. (2011) “Expression and purification of the C-terminal fragments of TRPV5/6 channels.” Protein Expr Purif. 80, 28-33.
  24. Vuister, G.W., Tjandra N., Grishaev, A., Shen, Y. & Grzesiek, S. (2011) “Measurement of structural constraints" in “Protein NMR Spectroscopy: Principal Techniques an Applications", G. Roberts & Lian, L-Y Eds. Wiley-Blackwell, Oxford.
  25. De Groot, T., Kovalevskaya, N.Z., Verkaart, S., Schilderink, N., Felici, M., Bindels, R.J.M., Vuister, G.W. & Hoenderop, J.G. (2011) “Molecular mechanisms of calmodulin action on TRPV5 and modulation by parathyroid hormone.”, Mol. Cell. Biol. 31, 2845-53.
  26. Breukels, V., Konijenberg, A., Nabuurs, S.M., Doreleijers, J.F., Kovalevskaya, N.V. & Vuister, G.W. (2011) “Overview on the Use of NMR to Examine Protein Structure”, Current Protocols in Protein Science, 17.5.1-17.5.44.
  27. Breukels, V. & Vuister, G.W. (2010) “Binding of calcium is sensed structurally and dynamically throughout the second calcium-binding domain of the sodium/calcium exchanger”, Proteins 78, 1813-24.
  28. Duchardt, F. Ruttekolk, I., Hufnagel, H, Fischer, R., van den Heuvel, M., Löwik, D., Vuister, G.W., Fotin-Mleczek, M., Wiesmüller, K-H. & Brock, R. (2009) “A cell-penetrating peptide derived from human lactoferrin”, J. Biol. Chem. 284, 36099-108.
  29. Doreleijers, J.F., Vranken, W., Schulte, C., Lin, J., Penkett, C., Vuister, G.W., Vriend, G., Markley, J.L. & Ulrich, E.L. (2009) “The NMR Restraints Grid (NRG) at BMRB for 4,411 protein and nucleic acid PDB entries”, J. Biomol. NMR 45, 389-96.
  30. Rosato, A., Bagaria, A., Baker, D., Bardiaux, B., Cavalli, A., Doreleijers, J.F., Giachetti, A., Guerry, P., Güntert, P., Herrmann, T., Huang, Y.J., Jonker, H.R., Mao, B., Malliavin, T.E., Montelione, G.T., Nilges, M., Raman, S., van der Schot, G., Vranken, W.F., Vuister GW & Bonvin A.M. (2009), “CASD-NMR: critical assessment of automated structure determination by NMR” Nature Methods 6, 625-6.
  31. Hilge, M., Aelen, J.M.A., Foarce, A., Perrakis, A. & Vuister, G.W. (2009), “Ca2+ regulation in the Na+/Ca2+ exchanger features a dual electrostatic switch mechanism”, Proc. Natl. Acad. Sci. U.S.A. 106, 14333-8.
  32. Johnson, E., Bruschweiler-Li, L., Showalter, S.A., Vuister, G.W., Zhang, F. & Bruschweiler, R. (2008) “Structure and Dynamics of Ca2+-Binding Domain 1 of the Na+/Ca2+ Exchanger in the Presence and Absence of Ca2+”, J. Mol. Biol. 377, 945-55.
  33. Van den Berk, L.C.J., Landi, E., Walma, T., Vuister, G.W., Dente, L. & Hendriks, W.J.A.J. (2007) “Modulation of PTP-BL PDZ2 binding specificity through an allosteric intramolecular PDZ1-PDZ2 interaction”, Biochemistry 46, 13629-13637.
  34. Maillard, J., Spronk, C.A.E.M, Buchanan, G., Lyall, V., Richardson, D.J., Palmer, T., Vuister, G.W. & Sargent, F (2007) “Escherichia Coli NapD, a Tat proofreading chaperone with anti-transport activity”, Proc. Natl. Acad. Sci. U.S.A. 104, 15641-15646.
  35. Hilge, M., Aelen, J.M.A., Perrakis, A. & Vuister, G.W. (2007) “Structural basis for Ca2+ regulation in the Na+/Ca2+ exchanger.” Annals N.Y. Acad. Sci. 1099, 7-15.
  36. Gianni, S., Geirerhaas, C.D., Calosci, N., Jemth, P., Vuister, G.W., Travaglini-Allocatelli, C., Vendruscolo, M. & Brunori, M. (2007) “A PDZ domain recapitulates a unifying mechanism for protein folding”, Proc. Natl. Acad. Sci. U.S.A. 104, 128-133.
  37. Gianni, S., Walma, T., Arcovito, A., Calosci, N., Bellelli, A., Engstöm, Å., Travaglini-Allocatelli, C., Brunori, M., Jemth, P. & Vuister, G.W. (2006) “Demonstration of Long-Range Interactions in a PDZ Domain by NMR, Kinetics, and Protein Enginering”, Structure 14, 1801-1809.
  38. Hilge, M., Aelen, J.M.A. & Vuister, G.W. (2006) “Ca2+-regulation in the Na+/Ca2+ exchanger involves two Markedly Different Ca2+ Sensors”, Mol. Cell 22, 15-25.
  39. Van Ingen, H., Vuister, G.W., Wijmenga, S.S., Tessari, M. (2006) “CEESY: characterizing the conformation of unobservable protein states”, J. Am. Chem. Soc. 128, 3856-3857.
  40. Van Ingen, H., Baltussen, M.A.H, Aelen, J. & Vuister, G.W. (2006) “Role of Structural and Dynamical Plasticity in Sin3: The Free PAH2 Domain is a Folded Module in mSin3B”, J. Mol. Biol. 358, 485-497.
  41. Nabuurs, S, Spronk, C.A.E.M., Vuister, G.W. & Vriend, G. (2006) “Traditional Biomolecular Structure Determination by NMR Spectroscopy Allows for Major Errors”, PLoS Comput. Biol. 2, e9.
  42. Nabuurs, S, Krieger, E., Spronk, C.A.E.M., Nederveen, A.J, Vriend, G., & Vuister, G.W. (2005) “Definition of a new information-based per-residue quality parameter”, J. Biomol. NMR 33, 123-134.
  43. Duquesne, A., de Ruijter, M., Brouwer, J., Drijfhout, J.W., Nabuurs, S.N., Spronk, C.A.E.M., Vuister, G.W., Ubbink, M. & Canters, G.W. (2005) “Solution structure of the second PDZ domain of the neuronal adaptor protein X11a and its interaction with the C-terminal peptide of the human Copper Chaperone for Superoxide dismutase”, J. Biomol. NMR 32, 209-218.
  44. Gianni, S., Travaglini-Allocatelli, C., Calosci, N., Aelen, J.M.A., Vuister, G.W., & Brunori, M. (2005) “Kinetic folding mechanism of PDZ2 from PTP-BL”, Protein. Eng. Des. Sel. 18, 389-395.
  45. Spronk, C.A.E.M., Nabuurs, S.B., Vriend, G. & Vuister, G.W. (2004) “Validation of High-Resolution NMR-Structures”, Prog. NMR Spectr. 45, 315-337.
  46. van den Berg, L.C.J., van Ham, M.A., te Lindert, M.M., Walma, T., Aelen, J.M.A., Vuister, G.W. & Hendriks, W.J.A.J. (2004) “The Interaction of PTP-BL PDZ domains with RIL: An enigmatic role for the RIL LIM domain, Mol. Biol. Reports 31, 203-215.
  47. Kloks, C.P.A.M., Tessari, M., Vuister, G.W., & Hilbers, C.W. (2004) “Backbone dynamics and equilibrium between the native state and a partially unfolded state”, Biochemistry 43, 10237-10246.
  48. Nabuurs, S.B., Spronk, C.A.E.M., Vriend, G. & Vuister, G.W. (2004) “Concepts and tools for validation of NMR data and structures”, Concepts in Magn. Reson. 22A, 90-105.
  49. Harrold A. van den Burg, H.A., Spronk, C.A.E.M., Boeren, S., Kennedy, M.A., Visser, J.P.C., Vuister, G.W., de Wit, P.J.G.M., & Vervoort, J. (2004) “Binding of the AVR4 elicitor of Cladosporium fulvum to chitotriose units is facilitated by positive allosteric protein-protein interactions”, J. Biol. Chem. 279, 16786-16796.
  50. Nabuurs, S.B., Nederveen, A.J., Vranken, W., Doreleijers, J.F., Bonvin, A.M.J.J., Vuister, G.W., Vriend, G. & Spronk, C.A.E.M. (2004) “DRESS, a Database of REfined Solution nmr Structures”, Proteins, Struct., Func., Genet. 45, 483-486.
  51. Ingen, H. van, Lasonder, E., Jansen, J.F.A., Kaan, A., Spronk, C.A.E.M., Stunnenberg, H.G & Vuister G.W. (2004) “Extension of the binding motif of the Sin3 Interacting Domain of the Mad-family proteins”, Biochemistry 43, 46-53.
  52. Walma, T., Aelen, J.M.A., Nabuurs, S.B., van den Berk, L., Oostendorp, M., Hendriks, W. & Vuister, G.W. (2004) “A closed binding pocket and global destabilization modify the binding properties of an alternatively spliced form of the second PDZ domain of PTP-BL”, Structure 12, 11-20.
  53. Wingens, M., Walma, T., van Ingen, H., Stortelers, C., van Leeuwen, J.E.M., van Zoelen, E.J.J. & Vuister, G.W. (2003) “Structural analysis of an EGF/TGFa chimera with unique ERBb binding specificity”, J. Biol. Chem. 278, 39114-39123.
  54. Nabuurs, S.B., Spronk, C.A.E.M, Krieger, E., Maassen, H., Vriend, G. & Vuister, G.W. (2003) “Quantitative evaluation of experimental NMR restraints”, J. Am. Chem. Soc. 125, 12026-12034.
  55. Hilge, M, Siegal, G., Vuister, G.W., Guntert, P., Gloor, S.M. & Abrahams, J.P. (2003) “ATP-induced conformational changes of the nucleotide binding domain of Na,K-ATPase”, Nature Struct. Biol. 10, 468-474.
  56. Spronk, C.A.E.M., Nabuurs, S.B., Bonvin, A.M.J.J., Krieger, E., Vuister, G.W. & Vriend, G. (2003), “The precision of NMR structure ensembles revisited”, J. Biomol. NMR 25, 225-234.
  57. Ingen, H. van,. Tessari, M. & Vuister, G.W (2002) “A 3D double-sensitivity enhanced X-filtered TOCSY-TOCSY experiment”, J. Biomol. NMR 24, 155-160.
  58. Ingen, H. van, Vuister, G.W. & Tessari, M. (2002), “A two-dimensional artifact from asynchronous decoupling”, J. Magn. Reson 156, 258-261.
  59. Spronk, C.A.E.M., Linge, J.P. & Hilbers C.W. & Vuister, G.W. (2002), “Improving the quality of protein structures derived by NMR spectroscopy”, J. Biomol. NMR 22, 281-289.
  60. Walma, T., Spronk, C.A.E.M., Tessari, M., Aelen, J.M.A., Schepens, J., Hendriks, W. & Vuister, G.W. (2002) “Structure, Dynamics and Binding Characteristics of the Second PDZ Domain of PTP-BL”, J. Mol. Biol 316, 1101-1110.
  61. Kloks, P.A.M., Spronk, C.A.E.M., Tessari, M., Vuister, G.W., Grzesiek, S. & Hilbers C.W. (2002) "Solution Structure and Backbone Dynamics of the Cold-Shock Domain of Human YB-1", J. Mol.Biol. 316, 317-326.
  62. Spronk, C.A.E.M., Jansen, J.F.A., Tessari, M., Kaan, A.M., Aelen, J.M.A., Lasonder, E., M., Stunnenberg, H.G & Vuister, G.W (2001) "Sequence-specific assignment of the PAH2 domain of Sin3B free- and bound to Mad1", J. Biomol. NMR 19, 377-378.
  63. Spronk, C.A.E.M., Tessari, M., Kaan, A.M., Jansen, J.F.A., Vermeulen, M., Stunnenberg, H.G & Vuister, G.W. (2000) "The Mad1-Sin3B interaction involves a novel helical fold", Nature Struct. Biol. 7, 1100-1104.
  64. Tessari, T. & Vuister, G.W. (2000) “A novel experiment for the quantitative measurement of CSA(1HN)/CSA(15N) cross-correlated relaxation in 15N-labeled proteins”, J. Biomol. NMR 16, 171-174.
  65. Whitehead, B., Tessari, M., Carotenuto, A., van Bergen en Henegouwen, P.M.P. & Vuister, G.W. (1999) “The EH1 domain of Eps15 is structurally classified as a member of the S100 subclass of EF-hand-containing proteins, Biochemistry 38, 11271-11277
  66. Carotenuto, A., Tessari, M., Whitehead, B., Aelen, J.M.A., van Bergen en Henegouwen, P.M.P., & Vuister, G.W. (1999) “Sequence-specific 1H, 13C and 15N assignment and secondary structure of the apo EH2 domain of mouse Eps15”, J. Biomol. NMR 14, 97-98.
  67. Rubinstenn, G., Vuister, G.W., Zwanenburg, N., Hellingwerf, K.J., Boelens, R., & Kaptein, R. (1999) “NMR experiments to study photo-intermediates: Application to the Photoactive Yellow Protein”, J. Magn. Reson. 137, 443-447.
  68. Vuister, G.W., Tessari, M., Karimi-Nejad, Y., & Whitehead, B. (1999) “Pulse Sequences for Measuring Coupling Constants” in “Modern Techniques in Protein NMR 16”, Berliner, L.J & Krishna, N.R (Eds.), Plenum Publishing Corporation, New York, 195-257.
  69. Pineda-Lucena, A., Vuister, G.W., Hilbers, C.W. (1999) “Sequence-specific 1H, 13C and 15N assignment of the single-stranded DNA-binding protein of the bacteriophage f29” J. Biomol. NMR 13, 303-304.
  70. Whitehead, B., Tessari, M., Versteeg, H.H., van Delft, S., van Bergen en Henegouwen, P.M.P., & Vuister, G.W. (1998) “Sequence-specific 1H, 13C and 15N assignment of the EH1 domain of mouse Eps15”, J. Biomol. NMR 12, 465-466.
  71. Kloks, C.P.A.M., Hoffmann, A., Ominchinski, J.G., Vuister, G.W., Hilbers, C.W., & Grzesiek, S. (1998) “Resonance Assignment and Secondary Structure of the Cold Shock Domain of the Human YB-1 Protein”, J. Biomol. NMR 12, 463-464.
  72. Reinking, J.L., Gentile, L.N., Tessari, T., Vuister, G.W. & Nicholson, L.K. (1998) “Mechanisms of Regulation in the Regulatory Apparatus of pp60c-Src” J. Biomol. Struct. & Dynamics 16, 53-62.
  73. Düx, P.E., Rubinstenn, G., Vuister, G.W., Boelens, R., Mulder, F.A.A., Hård, K., Hoff, W.D., Kroon, A.R., Crielaard, W., Hellingwerf, K.J. & Kaptein, R. (1998) “Solution structure and backbone dynamics of the photoactive yellow protein”, Biochemistry 37, 12689-12699.
  74. Rubinstenn, G., Vuister, G.W., Mulder, F.A.A., Düx, P.E., Boelens, R., Hellingwerf, K.J. & Kaptein, R. (1998) The long-lived intermediate of the Photoactive Yellow Protein photocycle is disordered in solution”, Nature Struct. Biol. 5, 568-570.
  75. Düx, P., Whitehead, B., Boelens, R., Kaptein, R. & Vuister, G.W. (1997) “Measurement of 15N-1H Coupling Constants in Uniformily 15N Labeled Proteins. Application to the Photoactive Yellow Protein”, J. Biomol. NMR 10, 301-306.
  76. Tessari, M., Gentile, L., Taylor, S.J., Shalloway, D., Nicholson, L. & Vuister, G.W. (1997) “Heteronuclear NMR studies of the combined SH3-SH2 domains of pp60 c-Src. The effects of phosphopeptide binding”, Biochemistry 36, 14561-14571.
  77. Whitehead, B., Tessari, M., Düx, P., Boelens, R., Kaptein, R. & Vuister, G.W. (1997) “An 15N-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. Biomol. NMR 9, 313-316.
  78. Tessari, M., Mulder, F., Boelens, R. & Vuister, G.W. (1997) “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. Reson. 127, 128-133.
  79. Tessari, M., Vis, H., Boelens, R., Kaptein, R. & Vuister, G.W. (1997) “Quantitative measurement of relaxation interference effects between 1HN CSA and 1H-15N dipolar interaction: correlation with secondary structure”, J. Am. Chem. Soc. 119, 8985-8990.
  80. Vuister, G.W., Knegtel, R.M.A. & Gincel, E. (1996) “DNA-binding by Heat-Shock Transcription Factors”, Biological Structure and Dynamics, Proceedings of the Ninth Conversation, State University of New York, Albany, NY,1995, Sarma, R.H. & Sarma, M.H. (Eds.) Adenine Press 1996, pp 91-107.
  81. Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu, G. Pfeifer, J. & Bax, A. (1995) “NMRPipe: a Multidimensional Spectral Processing System Based on UNIX Pipes”, J. Biomol. NMR 6, 277-293.
  82. Wang, A.C., Lodi, P.J, Qin, J., Vuister, G.W., Gronenborn, A.M. & Clore, G.M. (1994) “An Efficient Triple Resonance Experiment for Proton-Directed Sequential Backbone Assignment of Medium-Sized Proteins”, J. Magn. Reson. B 105, 196-198.
  83. Vuister, G.W., Kim, S-.J., Orosz, A., Marquardt, J., Wu, C. & Bax, A. (1994) “Solution Structure of the DNA-Binding Domain of Drosophila Heat Shock Transcription Factor”, Nature Struct. Biol. 1, 605-614.
  84. Vuister, G.W., Kim, S-.J., Wu, M. & Bax, A. (1994) “2D and 3D NMR Study of Phenylalanine Residues in Proteins by Reverse Isotopic Labeling”, J. Am. Chem. Soc. 116, 9206-9210.
  85. Bax, A., Delaglio F., Grzesiek, S. & Vuister, G.W. (1994) “Resonance Assignment of Methionine Methyl Groups and c3 Angular Information from Long Range Proton-Carbon and Carbon-Carbon J Correlation in a Calmodulin-Peptide Complex” J. Biomol. NMR 4, 787-797.
  86. Garrett, D.S., Kuszewski, J., Hancock, T., Lodi, P.J., Vuister, G.W., Gronenborn, A.M. & Clore, G.M. (1994) “The Impact of Direct Refinement Against Three-bond HN-CaH Coupling constants on Protein Structure Determination by NMR” J. Magn. Reson. B 104, 99-103.
  87. Vuister, G.W., Kim, S.J., Wu, C. & Bax, A (1994) “NMR Evidence for Similarities Between the DNA-Binding Regions of Drosophila melanogaster Heat Shock Factor and Helix-Turn-Helix and HNF-3/fork head Families of Transcription Factors” Biochemistry 33, 10-16.
  88. Vuister, G.W. & Bax, A. (1994) “Measurement of Four-bond HN-Ha J Couplings in Staphyloccal Nuclease” J. Biomol. NMR 4, 193-200.
  89. Bax, A., Vuister, G.W., Grzesiek, S., Delaglio, F., Wang, A.C., Tschudin, R. & Zhu, G. (1994) “Measurement of Homo- and Heteronuclear J Couplings from Quantitative J Correlation”, in James, T.L. & Oppenheimer, N.J. (eds) Methods in Enzymology 239, 79-105.
  90. Vuister, G.W. & Bax, A. (1993) “Measurement of Two- and Three-bond Proton to Methyl Carbon J Couplings in Proteins Uniformly Enriched in 13C” J. Magn. Reson. B 102, 228-231.
  91. Kleywegt, G.J., Vuister, G.W., Padilla, A., Knegtel, R.M.A., Boelens, R. & Kaptein, R. (1993) “Computer-Assisted Assignment of Homonuclear 3D NMR Spectra of Proteins. Application to Pike Parvalbumin III” J. Magn. Reson. B 102, 166-176.
  92. Grzesiek, S., Vuister, G.W. & Bax, A. (1993) “A Simple and Sensitive Experiment for Measurement of JCC Couplings Between Backbone Carbonyl and Methyl Protons in Isotopically Enriched Proteins”, J. Biomol. NMR 3, 487-493.
  93. Vuister, G.W. & Bax, A. (1993) “Quantitative J Correlation: A New Approach for Measuring Homonuclear Three-Bond J(HNHa) Coupling Constants in 15N-Enriched Proteins”, J. Am. Chem. Soc. 115, 7772-7777.
  94. Vuister, G.W., Wang, A.C. & Bax, A. (1993) “Measurement of Three-Bond Nitrogen-Carbon Couplings in Proteins Uniformly Enriched in 15N and 13C” J. Am. Chem. Soc. 115, 5334-5335.
  95. Vuister, G.W., Yamazaki, T., Torchia, D.A. & Bax, A. “Measurement of Two- and Three-Bond 13C-1H J Couplings to the C¬d Carbons of Leucine Residues in Staphylococcal Nuclease” (1993) J. Biomol. NMR 3, 297-306.
  96. Vuister, G.W., Clore, G.M., Gronenborn, A.M., Powers, R., Garrett, D.S., Tschudin, R. & Bax, A. “Increased Resolution and Improved Spectral Quality in Four-Dimensional 13C/13C Separated HMQC-NOESY-HMQC Spectra Using Pulsed Field Gradients” (1993) J. Magn. Reson. B 101, 210-213.
  97. Vuister, G.W., Delaglio, F. & Bax, A. “The Use of 1J¬CaHa Coupling Constants as a Probe for Protein Backbone Conformation” (1993) J. Biomol. NMR 3, 67-80.
  98. Ruiz-Cabello, J., Vuister, G.W., Moonen, C.T.W., Van Gelderen, P. & Van Zijl, P.C.M. “Gradient-Enhanced Heteronuclear Correlation Spectroscopy. Theory and Experimental Aspects.” (1992), J. Magn. Reson. 100, 282-302.
  99. Vuister, G.W., Delaglio, F. & Bax, A. “An Emperical Correlation Between 1J¬CaHa and Protein Backbone Conformation” (1992) J. Am. Chem. Soc. 114, 9674-9675.
  100. Vuister, G.W., Ruiz-Cabello, J. & van Zijl, P.C.M. “Gradient-Enhanced Muliple-Quantum Filter (ge-MQF). A Simple way for Obtaining Single-Scan Phase-Sensitive HMQC Spectra” (1992) J. Magn. Reson. 100, 215-220.
  101. Vuister, G.W. & Bax, A. “Measurement of Two-Bond JCOHa Coupling Constants in Proteins Uniformly Enriched in 13C” (1992) J. Biomol. NMR 2, 401-405.
  102. Vuister, G.W. & Bax, A. “Resolution Enhancement and Spectral Editing of Uniformly 13C Enriched Proteins by Homonuclear Broadband 13C Decoupling.” (1992) J. Magn. Reson. 98, 428-435.
  103. Vuister, G.W., Boelens, R., Kaptein, R., Burgering, M. & Van Zijl, P.C.M. “Gradient-Enhanced 3D NOESY-HMQC Spectroscopy”, (1992) J. Biomol. NMR 2, 301-305.
  104. de Waard, P., Leeflang, B.R., Vliegenthart, J.F.G., Boelens, R., Vuister, G.W. & Kaptein, R. “Application of 2D and 3D Experiments to the Conformational Study on a Diantennery Oligosaccharide” (1992) J. Biomol. NMR 2, 211-226.
  105. Moonen, C.T.W., Van Gelderen, P., Vuister, G.W. & Van Zijl, P.C. M. “Gradient-Enhanced Exchange Spectroscopy (GEXSY)”, (1992) J. Magn. Reson. 97, 419-425.
  106. Vuister, G.W., Boelens, R., Padilla, A. & Kaptein, R. “Statistical Analysis of Double NOE Transfer Pathways in Proteins as Measured in 3D NOE-NOE Spectroscopy”, (1991) J. Biomol. NMR 1, 421-438.
  107. Vuister, G.W., Boelens, R., Kaptein, R., Hurd, R.E., John, B. & Van Zijl, P.C.M “Gradient-Enhanced HMQC and HSQC spectroscopy. Applications to 15N labeled Mnt repressor in 1H2O”, (1991) J. Am. Chem. Soc. 113, 9688-9690.
  108. Vuister, G.W. “Homonuclear Three-Dimensional NMR Spectroscopy of Biomolecules”, (1991), Ph.D. Thesis, Utrecht, The Netherlands.
  109. de Waard, P., Boelens, R., Vuister, G.W., & Vliegenthart, J.F.G. “Structural Studies by 1H/13C Two-Dimensional and Three-Dimensional HMQC-NOE at Natural Abundance on Complex Carbohydrates” (1990) J. Am. Chem. Soc. 112, 3232-3234.
  110. Breg, J.N., Boelens, R., Vuister, G.W. & Kaptein, R. “3D NOE-NOE Spectroscopy of Proteins. Observation of Sequential 3D NOE Cross Peaks in Arc Repressor” (1990) J. Magn. Reson. 87, 646-651.
  111. Padilla, A., Vuister, G.W., Boelens, R., Kleywegt, G.J., Cavé, A., Parello, J. & Kaptein, R. "Homonuclear Three-Dimensional 1H NMR Spectroscopy of Pike Parvalbumin. Comparison of Short and Medium Range NOEs from 2D and 3D Spectra" (1990) J. Am. Chem. Soc. 112, 5024-5030.
  112. Vuister, G.W., Boelens, R., Padilla, A., Kleywegt, G.J. & Kaptein, R. "Assignment Strategies in Hononuclear Three-Dimensional 1H NMR Spectra of Proteins" (1990) Biochemistry 29, 1829-1839.
  113. Rullmann, J.A.C., Boelens, R., Lamerichs, R.M.J.N., Vuister, G.W. & Kaptein, R. “NMR Studies of Proteins and Protein-DNA interactions” (1989) in Modeling of Molecular Structures and Properties, Proceedings of the 44th International Meeting of Physical Chemistry, Ed. J. L. Rivail, Elsevier, Amsterdam, 661-678.
  114. Boelens, R., Vuister, G.W., Padilla, A., Kleywegt, G.J., de Waard, P., Koning, T.M.G. & Kaptein, R. "Three-Dimensional NMR Spectroscopy of Biomolecules" (1989) Proceedings of the Sixth Conversation in the Discipline Biomolecular Stereodynamics, State University of New York at Albany, June 06-10, 1989, 63-81.
  115. Boelens, R., Vuister, G.W., Koning, T.M.G. & Kaptein, R. "The Observation of Spin-Diffusion in Biomolecules by 3D NOE-NOE Spectroscopy" (1989) J. Am. Chem. Soc. 111, 8525-8526.
  116. Vuister, G.W., de Waard, P., Boelens, R., Vliegenthart, J.F.G. & Kaptein, R. "The Use of 3D NMR in Structural Studies of Oligosaccharides" (1989) J. Am. Chem. Soc. 111,772-774.
  117. Vuister, G.W., Boelens, R. & Kaptein, R. "Nonselective Three-Dimensional NMR Spectroscopy. The 3D NOE-HOHAHA Experiment" (1989) J. Magn. Reson. 80, 176-185.
  118. Mayo, K.H., Schussheim, A., Vuister, G.W., Boelens, R., Kaptein, R., Engelhard, M. & Hess, B. "Mobility and Solvent Exposure of Aromatic Residues in Bacteriorhodopsin Investigated by 1H-NMR and Photo-CIDNP-NMR Spectroscopy" (1988) FEBS Letters 235, 163-168.
  119. Endo, T., Oya, M., Kaptein, R., Vuister, G.W., Kihara, H., Mohri, N., Tanaka,S & Ohno, M. "Proton NMR Resonance Assignments and Surface Accessibility of the Tryptophan Residues of a Dimeric Phospholipase A2 from Trimeresurus flavoviridis" (1988) FEBS Letters 230, 57-60.
  120. Vuister, G.W. & Boelens, R. "Three-Dimensional J-Resolved NMR Spectroscopy" (1987) J. Magn. Reson. 73, 328-333.
  121. Kemmink, J., Vuister, G.W., Boelens, R., Dijkstra, K. & Kaptein, R. "Nuclear Spin Coherence Transfer in Photochemical Reactions" (1986) J. Am. Chem. Soc. 108, 5631-5633.


See my LISCB Page to view my research.


Prof. Vuister welcomes applications of PhD students that are interested in structural projects or NMR-related methods development.

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