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- W1978391681 abstract "Abstract Hemopeptide 1–65 was cleaved from horse heart cytochrome c by cyanogen bromide and purified by exclusion chromatography. Although the intrinsic viscosity of the hemopeptide is intermediate between that of a compact sphere and a random coil, the ultraviolet circular dichroic spectrum indicates no significant amount of secondary structure. A variety of chemical and spectral measurements indicate that two histidyl residues of the hemopeptide are coordinated with the heme iron, that the indole ring of tryptophan 59 is one-third exposed, that the heme moiety is two-thirds exposed, and that tyrosyl 48 and the third histidyl residue are completely exposed. It was concluded that the hemopeptide has a relatively open conformation quite different from its conformation in the native protein." @default.
- W1978391681 created "2016-06-24" @default.
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- W1978391681 date "1972-01-01" @default.
- W1978391681 modified "2023-09-26" @default.
- W1978391681 title "The structure of hemopeptide 1–65 from cytochrome c" @default.
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- W1978391681 doi "https://doi.org/10.1016/0003-9861(72)90124-5" @default.
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