Probing the Effect of Mutations on Cytochrome c Stability
Francesco Agueci, Fabio Polticelli, Federica Sinibaldi, Maria Cristina Piro, Roberto Santucci and Laura Fiorucci
Pages 335-339 (5)
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.
Cytochrome c, guanidinium chloride unfolding, protein stability, circular dichroism, mutagenesis
Department of Experimental Medicine and Biochemical Sciences, “Tor Vergata” University, via Montpellier 1, 00133 Roma, Italy.