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Autor:
Rothfuss MT; Department of Chemistry and Biochemistry, University of Montana, Missoula, Montana 59812, United States., Becht DC; Department of Chemistry and Biochemistry, University of Montana, Missoula, Montana 59812, United States., Zeng B; Center for Biomolecular Structure and Dynamics, University of Montana, Missoula, Montana 59812, United States., McClelland LJ; Center for Biomolecular Structure and Dynamics, University of Montana, Missoula, Montana 59812, United States.; Division of Biological Sciences, University of Montana, Missoula, Montana 59812, United States., Yates-Hansen C; Center for Biomolecular Structure and Dynamics, University of Montana, Missoula, Montana 59812, United States., Bowler BE; Department of Chemistry and Biochemistry, University of Montana, Missoula, Montana 59812, United States.; Center for Biomolecular Structure and Dynamics, University of Montana, Missoula, Montana 59812, United States.
Publikováno v:
Journal of the American Chemical Society [J Am Chem Soc] 2023 Oct 25; Vol. 145 (42), pp. 22979-22992. Date of Electronic Publication: 2023 Oct 10.
Publikováno v:
Journal of the American Chemical Society. 131(3)
Unlike most ordered molecular systems, globular proteins exhibit a temperature of maximum stability, implying that the structure can be disrupted by cooling. This cold denaturation phenomenon is usually linked to the temperature-dependent hydrophobic