## 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
Empirical scale of conformational entropy for protein folding
β Scribed by M.J.E. Sternberg; S.D. Pickett; J.S. Chickos
- Publisher
- Elsevier Science
- Year
- 1993
- Tongue
- English
- Weight
- 126 KB
- Volume
- 11
- Category
- Article
- ISSN
- 0263-7855
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π SIMILAR VOLUMES
## 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.
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
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