## 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 sideβchain conformers in the native structure. Conformational entropy changes can be found by comparing the number of ac
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Empirical Scale of Side-Chain Conformational Entropy in Protein Folding
β 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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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
AN ANALYSIS OF SIDE-CHAIN CONFORMATION I
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