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.
Содержание
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.
Об авторе
Derek J. Chadwick and Kate Widdows are editors for Protein Conformation and other scientific titles.
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