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 des matières
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.
A propos de l’auteur
Derek J. Chadwick and Kate Widdows are editors for Protein Conformation and other scientific titles.
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