Titlebook: Statistical Mechanics, Protein Structure, and Protein Substrate Interactions; Sebastian Doniach Book 1994 Springer Science+Business Media

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Book 1994has led to a new branch of biochemistry in which quantitative measurements can be made assessing the influence of a given amino acid on the function of a biological molecule. A third factor, resulting from the exponential increase in computing power available to researchers, has been the emergence o

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Patricia A. Jennings,H. Jane Dyson,Peter E. Wright

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Apostolos G. Gittis,Wesley E. Stites,Eaton E. Lattman

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J. C. Smith,P. Calmettes,D. Durand,M. Desmadril,S. Furois-Corbin,G. R. Kneller,B. Roux

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Ron Elber,Adrian Roitberg,Carlos Simmerling,Robert Goldstein,Gennady Verkhivker,Haiying Li,Alex Ulit

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Hydrophobic Zippers: A Conformational Search Strategy for Proteinsle HP (H: hydrophobic, P: polar) copolymers in lattice models. In addition, we believe that the sequence of serial steps followed by the hydrophobic zippers construction process closely parallels the sequence of kinetic events in the fast stages of the folding processes of globular proteins.

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Computer-Supported Protein Structure Determination by NMRomic resolution could only be determined by X-ray diffraction techniques with protein single crystals (Blundell and Johnson, 1976). The introduction of nuclear magnetic resonance (NMR) spectroscopy as a technique for protein structure determination has made it possible to obtain structures at comparable resolution in solution (Wüthrich, 1986).