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Protein Conformation

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

ISBN: 978-0-470-51414-6 September 2007 282 Pages


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.