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Empirical Scale of Side-Chain Conformational Entropy in Protein Folding

✍ Scribed by Stephen D. Pickett; Michael J.E. Sternberg


Book ID
115626052
Publisher
Elsevier Science
Year
1993
Tongue
English
Weight
790 KB
Volume
231
Category
Article
ISSN
0022-2836

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πŸ“œ SIMILAR VOLUMES


Side-chain conformational entropy in pro
✍ Andrew J. Doig; Michael J. E. Sternberg πŸ“‚ Article πŸ“… 1995 πŸ› Cold Spring Harbor Laboratory Press 🌐 English βš– 475 KB

## Abstract An important, but often neglected, contribution to the thermodynamics of protein folding is the loss of entropy that results from restricting the number of accessible side‐chain conformers in the native structure. Conformational entropy changes can be found by comparing the number of ac

Estimates of the loss of main-chain conf
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The average contribution of conformational entropy for individual amino acid residues towards the free energy of protein folding is not well understood. We have developed empirical scales for the loss of the main-chain (torsion angles, and ) conformational entropy by taking its side-chain into accou