title: Protein conformational "annealing": binding to cytochrome c refolds the active site region of recombinant cytochrome c peroxidase.
abstract: When initially isolated with heme reconstitution, recombinant cytochrome c peroxidase molecules exhibit a conformation, revealed by visible spectra which observably differ from the corresponding holo proteins isolated from yeast. Binding yeast iso-1 cytochrome c to these recombinant cytochrome c peroxidases (either in solution or via an affinity column) catalyses a local refolding of the recombinant proteins to a form that is indistinguishable from the native (yeast) protein.
authors.affiliation: Department of Chemistry, University of Rochester, NY 14627.
authors.forename: R
authors.initials: R
authors.lastname: Hake
authors.forename: G
authors.initials: G
authors.lastname: McLendon
authors.forename: A F
authors.initials: AF
authors.lastname: Corin
mesh_terms: D001665:Binding Sites; D003574:Cytochrome c Group / Q000737:chemistry* / Q000378:metabolism; D003578:Cytochrome-c Peroxidase / Q000737:chemistry* / Q000378:metabolism; D004926:Escherichia coli / Q000201:enzymology*; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D013056:Spectrophotometry, Ultraviolet; D015003:Yeasts / Q000201:enzymology
chemical_list: D003574:Cytochrome c Group; D011994:Recombinant Proteins; D003578:Cytochrome-c Peroxidase