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- W2894803669 endingPage "20180244" @default.
- W2894803669 startingPage "20180244" @default.
- W2894803669 abstract "Although it is now relatively well understood how sequence defines and impacts global protein stability in specific structural contexts, the question of how sequence modulates the configurational landscape of proteins remains to be defined. Protein configurational equilibria are generally characterized by using various chemical denaturants or by changing temperature or pH. Another thermodynamic parameter which is less often used in such studies is high hydrostatic pressure. This review discusses the basis for pressure effects on protein structure and stability, and describes how the unique mechanisms of pressure-induced unfolding can provide unique insights into protein conformational landscapes." @default.
- W2894803669 created "2018-10-12" @default.
- W2894803669 creator A5020901311 @default.
- W2894803669 creator A5074482582 @default.
- W2894803669 date "2018-10-01" @default.
- W2894803669 modified "2023-10-18" @default.
- W2894803669 title "Lessons from pressure denaturation of proteins" @default.
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