Derek J. Chadwick & Kate Widdows 
Protein Conformation [PDF ebook] 

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.

Cuprins

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.

Despre autor

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