Chadwick / Widdows Protein Conformation

1. Auflage 2008
ISBN: 978-0-470-51415-3
Verlag: John Wiley & Sons
Format: PDF
Kopierschutz: Adobe DRM (»Systemvoraussetzungen)

E-Book, Englisch, 282 Seiten, E-Book

Reihe: Novartis Foundation Symposium

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.

Autoren/Hrsg.

Chadwick, Derek J.

Widdows, Kate

Inhaltsverzeichnis

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.