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Journal of the Royal Society interface, 2018-10, Vol.15 (147), p.20180244
Ort / Verlag
England
Erscheinungsjahr
2018
Quelle
MEDLINE
Beschreibungen/Notizen
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.