Article
Denatured state thermodynamics: residual structure, chain stiffness and scaling factors.
Journal of molecular biology - 31 Aug 2001
Hammack B N, Smith C R, Bowler B E
Abstract excerpt
A set of nine variants of yeast iso-1-cytochrome c with zero or one surface histidine have been engineered such that the N-terminal amino group is acetylated in vivo. N-terminal acetylation has been confirmed by mass spectral analysis of intact and proteolytically digested protein. The histidine-heme loop-forming equilibrium, under denaturing conditions (3 M guanidine hydrochloride), has been measured by pH...
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