Protein Conformation

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.

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 andan Approach to the Inverse Folding Problem (T. Blundell).Structural and Genetic Analysis of Electrostatic and OtherInteractions in Bacteriophage T4 Lysozyme (S. Dao-pin, etal.).Simulation Analysis of the Stability Mutants R96H ofBacteriophage T4 Lysozyme and I96A of Barnase (M. Karplus, etal.).Towards Time-Resolved Diffraction Studies with GlycogenPhosphorylase (E. Duke, et al.).The Application of Computational Methods to the Study of EnzymeCatalysis by Triose-Phosphate Isomerase and Stabilities of Variantsof Bacteriophage T4 Lysozyme (P. Kollman, et al.).Multidimensional Triple Resonance NMR Spectroscopy ofIsotopically Uniformly Enriched Proteins: A Powerful New Strategyfor Structure Determination (A. Bax, et al.).Six Years of Protein Structure Determination by NMRSpectroscopy: What Have We Learned?(K. Wüthrich).Index of Contributors.Subject Index.