Novartis Foundation Symposia, Band 161 1. Aufl.
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.
Partial table of contents: Mechanisms of Enzyme Catalysis from Crystal Structure Analyses (G. Schulz). Comparative Analysis of Protein Three-Dimensional Structures and an Approach to the Inverse Folding Problem (T. Blundell). Structural and Genetic Analysis of Electrostatic and Other Interactions in Bacteriophage T4 Lysozyme (S. Dao-pin, et al.). Simulation Analysis of the Stability Mutants R96H of Bacteriophage T4 Lysozyme and I96A of Barnase (M. Karplus, et al.). Towards Time-Resolved Diffraction Studies with Glycogen Phosphorylase (E. Duke, et al.). The Application of Computational Methods to the Study of Enzyme Catalysis by Triose-Phosphate Isomerase and Stabilities of Variants of Bacteriophage T4 Lysozyme (P. Kollman, et al.). Multidimensional Triple Resonance NMR Spectroscopy of Isotopically Uniformly Enriched Proteins: A Powerful New Strategy for Structure Determination (A. Bax, et al.). Six Years of Protein Structure Determination by NMR Spectroscopy: What Have We Learned? (K. Wüthrich). Index of Contributors. Subject Index.
Protein Conformation Chairman: F.M. Richards 1991 One of the major unsolved problems in biology and chemistry is how the amino acid sequence of a protein determines its three-dimensional structure, yet this structure is fundamental to the functioning and mechanism of action of enzymes, channels and receptors. Since the pioneering modelling work of Pauling in the 1940s and the X-ray structure determinations by Kendrew and Perutz in the 1960s, much structural information on proteins has been amassed. Several hundred protein structures have now been solved by X-ray crystallography and, more recently, NMR spectroscopy has had a significant impact on the study of structures of small proteins in solution. In this book, contributions from experts in the fields of X-ray crystallography, NMR spectroscopy, molecular modelling and protein engineering provide insight into current views on the protein folding problem and point to avenues for future progress. The use of molecular dynamics simulations to provide information about protein structure, dynamics and stability, and about protein—protein interactions, is discussed. Other topics focused on include enzyme catalysis, site-directed mutagenesis as a tool in studies of protein conformation and stability, and recent developments in multidimensional NMR methodology. Related Ciba Foundation Symposia No 159 Catalytic antibodies Chairman: W.P. Jencks 1991 ISBN 0 471 92962 X No 158 Host-guest molecular interactions: from chemistry to biology Chairman: I.O. Sutherland 1991 ISBN 0 471 92958 1 No 145 Carbohydrate recognition in cellular function Chairman: E. Ruoslahti 1989 ISBN 0 471 92307 9 No 119 Synthetic peptides as antigens Chairman: G.L. Ada 1986 ISBN 0 471 99838 9
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