Probing the effect of mutations on cytochrome C stability.
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.
Agueci
Francesco
F
Department of Experimental Medicine and Biochemical Sciences, Tor Vergata University, via Montpellier 1, Roma, Italy.
Polticelli
Fabio
F
Sinibaldi
Federica
F
Piro
Maria Cristina
MC
Santucci
Roberto
R
Fiorucci
Laura
L
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
C014059:CYC1 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; D045304:Cytochromes c; D019791:Guanidine