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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| Pubblicato in: | Proc Natl Acad Sci U S A |
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| Autori principali: | , , , , |
| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
National Academy of Sciences
1998
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| Soggetti: | |
| Accesso online: | 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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