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

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Book 1994irst, there has been the considerable growth in our ability to obtain atomic-resolution structural data for biological molecules in general, and proteins in particular. This is a result of advances in technique, both in x-ray crystallography, driven by the development of electronic detectors and of

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Circular Dichroism Stopped-Flow Studies of Folding Intermediatese molecule from exploring the entire conformational space and “force” it to reach the native conformation in an unexpectedly short time interval. Whether the intermediates appear along a unique folding pathway rather than along different possible pathways is still controversial. Yet, more and more e

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Goblet-Cells

A First-Order Phase Transition Between a Compact Denatured State and a Random Coil State in Staphylotions in macroscopic systems. In such transitions the protein exists in just two detectable states, native and denatured, separated by an eneregy barrier; all the intermediate states are unstable and only transiently populated. The two-state model has been extraordinarily successful in accounting fo

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Studies on “Hyperstable” Proteins: Crystallins from the Eye-Lens and Enzymes from Thermophilic Bactetion in terms of local structural changes or stabilization by “extrinsic factors” not encoded in the amino acid sequence. Such factors are, among others, specific metabolites, cofactors, ions and chaperones. No general strategies of stabilization have yet been established. However, certain increment

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