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• W2085924900 startingPage "1430" @default.
• W2085924900 abstract "We describe a specific modification of iso-1 cytochrome c which results in blocking a single free sulfhydryl group. The derivative differs from the unmodified protein by the introduction of a small, uncharged group, thus maintaining the same charge balance as the native protein. The modified protein, obtained by treatment of iso-1 cytochrome c with iodoacetamide, has an activity indistinguishable from that of the unmodified protein in the lactate dehydrogenase-cytochrome c reductase system from yeast and has the same stability toward denaturation by guanidine hydrochloride. The kinetics of fluorescence changes associated with the guanidine hydrochloride induced folding-unfolding transition for modified iso-1 cytochrome c (iso-1-AM) have been investigated throughout the transition zone by using stopped-flow mixing. The results are compared to those for the yeast isozyme, iso-2 cytochrome c. The main features of the fluorescence-detected folding kinetics are similar, as might be expected for homologous proteins; however, the limiting value of the fraction of fast refolding protein (alpha 2) below the transition zone is smaller for iso-1-AM (approximately 0.7) than for iso-2 (approximately 0.9)." @default.
• W2085924900 created "2016-06-24" @default.
• W2085924900 creator A5046029643 @default.
• W2085924900 creator A5089688050 @default.
• W2085924900 date "1983-03-15" @default.
• W2085924900 modified "2023-09-27" @default.
• W2085924900 title "Folding of yeast iso-1-AM cytochrome c" @default.
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• W2085924900 doi "https://doi.org/10.1021/bi00275a017" @default.
• W2085924900 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/6301549" @default.
• W2085924900 hasPublicationYear "1983" @default.
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