Zobrazeno 1 - 3
of 3
pro vyhledávání: '"35"'
Autor:
Skalicky JJ; Contribution from the Department of Chemistry, State University of New York at Buffalo, Buffalo, New York 14260, USA., Mills JL, Sharma S, Szyperski T
Publikováno v:
Journal of the American Chemical Society [J Am Chem Soc] 2001 Jan 24; Vol. 123 (3), pp. 388-97.
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
Publikováno v:
Journal of the American Chemical Society. 123(3)
We have characterized, for the first time, motional modes of a protein dissolved in supercooled water: the flipping kinetics of phenylalanyl and tyrosinyl rings of the 6 kDa protein BPTI have been investigated by NMR at temperatures between -3 and -1