title: Probing the effect of mutations on cytochrome C stability.
abstract: Although the tertiary structures of mitochondrial cytochromes c (cyts c) seem to be remarkably similar, there are variations in their amino acid sequences, stability and functional properties. GdnHCl-induced unfolding experiments on engineered yeast and horse cyt c were carried out with the aim to to clarify, at molecular level, some aspects concerning the stability of this class of proteins. The results obtained are discussed in the light of the three-dimensional structures of the two proteins.
authors.affiliation: Department of Experimental Medicine and Biochemical Sciences, Tor Vergata University, via Montpellier 1, Roma, Italy.
authors.forename: Francesco
authors.initials: F
authors.lastname: Agueci
authors.forename: Fabio
authors.initials: F
authors.lastname: Polticelli
authors.forename: Federica
authors.initials: F
authors.lastname: Sinibaldi
authors.forename: Maria Cristina
authors.initials: MC
authors.lastname: Piro
authors.forename: Roberto
authors.initials: R
authors.lastname: Santucci
authors.forename: Laura
authors.initials: L
authors.lastname: Fiorucci
mesh_terms: D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D000818:Animals; D045304:Cytochromes c / Q000187:drug effects / Q000235:genetics*; D004795:Enzyme Stability; D019791:Guanidine / Q000494:pharmacology; D006736:Horses; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011489:Protein Denaturation; D017510:Protein Folding; D017434:Protein Structure, Tertiary / Q000187:drug effects; D029701:Saccharomyces cerevisiae Proteins / Q000235:genetics
chemical_list: C014059:CYC1 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; D045304:Cytochromes c; D019791:Guanidine