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, F., Polticelli, F., Sinibaldi, F., Piro, M.c., Santucci, R., Fiorucci, L. (2007). Probing the effect of mutations on cytochrome c stability RID A-4573-2009. PROTEIN AND PEPTIDE LETTERS, 14(4), 335-339 [10.2174/092986607780363989 WC Biochemistry & Molecular Biology].

Probing the effect of mutations on cytochrome c stability RID A-4573-2009

POLTICELLI, Fabio;
2007-01-01

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.
2007
Agueci, F., Polticelli, F., Sinibaldi, F., Piro, M.c., Santucci, R., Fiorucci, L. (2007). Probing the effect of mutations on cytochrome c stability RID A-4573-2009. PROTEIN AND PEPTIDE LETTERS, 14(4), 335-339 [10.2174/092986607780363989 WC Biochemistry & Molecular Biology].
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11590/153652
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