Buffering the entropic cost of hydrophobic collapse in protein chains
- 8 December 2004
- journal article
- research article
- Published by AIP Publishing in The Journal of Chemical Physics
- Vol. 121 (22), 11501-11502
- https://doi.org/10.1063/1.1814079
Abstract
Direct inspection of high-resolution protein structures reveals that backbone dehydration promotes extra conformational freedom in the peptide bond, especially when the residue is not involved in secondary structure. The results imply a buffering effect that lowers the entropic cost of hydrophobic collapse.Keywords
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