Conformational dynamics of a biologically active three-fragment complex of horse cytochrome c.
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چکیده
منابع مشابه
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The previous studies have shown that (a) noncovalent interactions of the ferro-heme fragment of residues 1-38 and apoprotein (1-104) of horse cytochrome c simultaneously and specifically form two isomeric complexes, types I and II resembling the native protein (the redundant residues flexibly protruding from the ordered structure); (b) the type II form but not type I appears to bind to CO; and ...
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Conformational transitions of oxidized and reduced cytochrome c at various solvent conditions are summarized. Sorbitol stabilizes and NaCl destabilizes native cytochrome c structure against the acid denaturation. In the process of heating, NaCl more strongly stabilizes molten globular cytochtome c state than sorbitol in secondary structure region, but in heme region, sorbitol is stronger stabil...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1982
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.79.6.1825