Ciba Foundation Symposium 161 - Protein Conformation

Copyright © Ciba Foundation 1991

Ciba Foundation Symposium 161 - Protein Conformation

Editor(s): Derek J. Chadwick, Kate Widdows

Published Online: 28 SEP 2007

Print ISBN: 9780471929697

Online ISBN: 9780470514146

DOI: 10.1002/9780470514146

About this Book

Product Information

About The Product

How the amino acid sequence of a protein determines its three-dimensional structure is a major problem in biology and chemistry. Leading experts in the fields of NMR spectroscopy, X-ray crystallography, protein engineering and molecular modeling offer provocative insights into current views on the protein folding problem and various aspects for future progress.

Table of contents

    1. You have free access to this content
      Front Matter (pages i–xii)

    2. Introduction (pages 1–7)

      F. M. Richards

    3. Mechanisms of Enzyme Catalysis from Crystal Structure Analyses (pages 8–27)

      Georg E. Schulz

    4. Comparative Analysis of Protein Three-Dimensional Structures and an Approach to the Inverse Folding Problem (pages 28–51)

      Tom L. Blundell

    5. Structural and Genetic Analysis of Electrostatic and Other Interactions in Bacteriophage T4 Lysozyme (pages 52–62)

      S. Dao-Pin, H. Nicholson, W. A. Baase, X.-J. Zhang, J. A. Wozniak and B. W. Matthews

    6. Simulation Analysis of the Stability Mutants R96H of Bacteriophage T4 Lysozyme and I96A of Barnase (pages 63–74)

      Martin Karplust, Martine Prévost, Bruce Tidor and Shoshana Wodak

    7. Towards Time-Resolved Diffraction Studies with Glycogen Phosphorylase (pages 75–90)

      E. M. H. Duke, A. Hadfield, J. L Martin, I. J. Clifton, J. Hajdu, L. N. Johnson, G. P. Reid, D. R. Trentham, I. Bruce and G. W. J. Fleet

    8. The Application of Computational Methods to the Study of Enzyme Catalysis by Triose-Phosphate Isomerase and Stabilities of Variants of Bacteriophage T4 Lysozyme (pages 91–107)

      Peter A. Kollman, Valerie Daggett and Liem X. Dang

    9. Multidimensional Triple Resonance NMR Spectroscopy of Isotopically Uniformly Enriched Proteins: A Powerful New Strategy for Structure Determination (pages 108–135)

      Ad Bax, Mitsuhiko Ikura, Lewis E. Kay, Gaetano Barbato and Silvia Spera

    10. Six Years of Protein Structure Determination by NMR Spectroscopy: What Have we Learned? (pages 136–149)

      Kurt Wüthrich

    11. On Deriving Spatial Protein Structure from NMR or X-Ray Diffraction Data (pages 150–166)

      W. F. van Gunsteren, P. Gros, A. E. Torda, H. J. C. Berendsent and R. C. van Schaik

    12. NMR Spectroscopy and Protein Folding: Studies of Lysozyme and α-Lactalbumin (pages 167–189)

      Christopher M. Dobson

    13. Experimental Studies of Pathways of Protein Folding (pages 190–205)

      Robert L. Baldwin

    14. Protein Stability and Protein Folding (pages 206–221)

      Rainer Jaenicke

    15. Ca2+ Binding in Proteins of the Calmodulin Superfamily: Cooperativity, Electrostatic Contributions and Molecular Mechanisms (pages 222–236)

      Sture Forsén, Sara Linse, Torbjörn Drakenberg, Johan Kördel, Mikael Akke, Peter Sellers, Charlotta Johansson, Eva Thulin, Ingrid Andersson, Peter Brodin, Thomas Grundström, Nicholas J. Skelton and Walter J. Chazin

    16. Protein-Protein Interaction: An Analysis by Computer Simulation (pages 237–259)

      Stéphane Duquerroy, Jacqueline Cherfils and Joël Janin

    17. You have free access to this content
      Index of Contributors (pages 260–261)

    18. You have free access to this content
      Subject Index (pages 262–269)

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