On the entropy of protein folding
Open Access
- 1 March 1996
- journal article
- research article
- Published by Wiley in Protein Science
- Vol. 5 (3) , 507-510
- https://doi.org/10.1002/pro.5560050312
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.Keywords
Funding Information
- NIH ((GM48036-01))
- NSF ((MCB 9118687))
This publication has 55 references indexed in Scilit:
- The interpretation of protein structures: Estimation of static accessibilityPublished by Elsevier ,2004
- Environment and exposure to solvent of protein atoms. Lysozyme and insulinPublished by Elsevier ,2004
- Application of a Self-consistent Mean Field Theory to Predict Protein Side-chains Conformation and Estimate Their Conformational EntropyJournal of Molecular Biology, 1994
- Helix propensities of the amino acids measured in alanine‐based peptides without helix‐stabilizing side‐chain interactionsProtein Science, 1994
- Determination of α-Helix Propensity within the Context of a Folded ProteinJournal of Molecular Biology, 1994
- Contribution of Hydration to Protein Folding ThermodynamicsJournal of Molecular Biology, 1993
- α-Helix stability in proteinsJournal of Molecular Biology, 1992
- Contribution of hydration and non-covalent interactions to the heat capacity effect on protein unfoldingJournal of Molecular Biology, 1992
- Interior and surface of monomeric proteinsJournal of Molecular Biology, 1987
- The nature of the accessible and buried surfaces in proteinsJournal of Molecular Biology, 1976