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Probing the Effect of Mutations on Cytochrome c Stability

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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.

Keywords: Cytochrome c; circular dichroism; guanidinium chloride unfolding; mutagenesis; protein stability

Document Type: Research Article


Affiliations: Department of Experimental Medicine and Biochemical Sciences, “Tor Vergata” University, via Montpellier 1, 00133 Roma, Italy.

Publication date: 2007-04-01

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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