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
On the entropy of protein folding
β Scribed by George I. Makhatadze; Peter L. Privalov
- Publisher
- Cold Spring Harbor Laboratory Press
- Year
- 2008
- Tongue
- English
- Weight
- 484 KB
- Volume
- 5
- Category
- Article
- ISSN
- 0961-8368
No coin nor oath required. For personal study only.
β¦ Synopsis
Abstract
The failure to appreciate that the hydration of polar groups is a major contribution to the entropy of protein unfolding has led to considerable underestimates for the loss of configurational freedom when a protein chain folds.
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## Abstract We offer simple solutions to three kinematic problems that occur in the folding of proteins. We show how to construct suitably local elementary Monte Carlo moves, how to close a loop, and how to fold a loop without breaking the bond that closes it. Β© 2003 Wiley Periodicals, Inc. J Compu
The folded native state of a globular protein is noted to be marginally stabilized over the structureless unfolded state by various atomic/group interactions. Quantitative enumeration of these factors remains to be a difficult task to workers in the field. In this work we collect experimental inform