The pressure dependence of hydrophobic interactions is consistent with the observed pressure denaturation of proteins

Proteins can be denatured by pressures of a few hundred MPa. This finding apparently contradicts the most widely used model of protein stability, where the formation of a hydrophobic core drives protein folding. The pressure denaturation puzzle is resolved by focusing on the pressure-dependent trans...

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Veröffentlicht in:	Proc Natl Acad Sci U S A
Hauptverfasser:	Hummer, Gerhard, Garde, Shekhar, García, Angel E., Paulaitis, Michael E., Pratt, Lawrence R.
Format:	Artigo
Sprache:	Inglês
Veröffentlicht:	National Academy of Sciences 1998
Schlagworte:	Biological Sciences
Online-Zugang:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC19087/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/9465053/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.95.4.1552
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