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• W2040890941 abstract "The loop segment comprising residues 70-84 in mitochondrial cytochrome c serves to direct the polypeptide backbone to permit the functionally required heme Fe - S (Met-80) co-ordination. The primary sequence here is highly conserved, which is something rarely observed in surface loop segments and suggests that its purpose is more complex than its obvious structural role. The beta-II turn formed by Pro-76 and Gly-77 is postulated to be key to the redirection of the peptide backbone required to execute the loop. We assessed the importance of Pro-76 and Gly-77 by mutating 1 or both of these residues to alanine such that the range of allowable dihedral angles was altered, and this resulted in significant changes in physicochemical properties and biological activities. We observed structural perturbations using circular dichroism spectroscopy and thermal denaturation studies. Based on these changes, we propose that the Pro-76/Gly-77 beta-II turn precisely orients the 70s loop, not only to maintain the backbone orientation required for the formation of the axial heme ligand, but also to provide a complementary surface to physiological partners." @default.
• W2040890941 created "2016-06-24" @default.
• W2040890941 creator A5000461537 @default.
• W2040890941 creator A5044982378 @default.
• W2040890941 date "2007-06-01" @default.
• W2040890941 modified "2023-09-25" @default.
• W2040890941 title "Probing the role of the conserved β-II turn Pro-76/Gly-77 of mitochondrial cytochromec" @default.
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• W2040890941 doi "https://doi.org/10.1139/o07-049" @default.
• W2040890941 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/17612631" @default.
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