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. PROTEIN AND PEPTIDE LETTERS, 14(4), 335-339 [10.2174/092986607780363989].

Probing the effect of mutations on cytochrome c stability

SINIBALDI, FEDERICA;PIRO, MARIA CRISTINA;SANTUCCI, ROBERTO;FIORUCCI, LAURA
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
Pubblicato
Rilevanza internazionale
Articolo
Sì, ma tipo non specificato
Settore BIO/10 - BIOCHIMICA
English
Con Impact Factor ISI
Circular dichroism; Cytochrome c; Guanidinium chloride unfolding; Mutagenesis; Protein stability
Agueci, F., Polticelli, F., Sinibaldi, F., Piro, M.c., Santucci, R., Fiorucci, L. (2007). Probing the effect of mutations on cytochrome c stability. PROTEIN AND PEPTIDE LETTERS, 14(4), 335-339 [10.2174/092986607780363989].
Agueci, F; Polticelli, F; Sinibaldi, F; Piro, Mc; Santucci, R; Fiorucci, L
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2108/37717
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