Unifying microscopic mechanism for pressure and cold denaturations of proteins

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Abstract

We study the stability of globular proteins as a function of temperature and pressure through NPT simulations of a coarse-grained model. We reproduce the elliptical stability of proteins and highlight a unifying microscopic mechanism for pressure and cold denaturations. The mechanism involves the solvation of nonpolar residues with a thin layer of water. These solvated states have lower volume and lower hydrogen-bond energy compared to other conformations of nonpolar solutes. Hence, these solvated states are favorable at high pressure and low temperature, and they facilitate protein unfolding under these thermodynamical conditions.

Original languageEnglish (US)
Article number048104
JournalPhysical Review Letters
Volume109
Issue number4
DOIs
StatePublished - Jul 27 2012
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Physics and Astronomy(all)

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