Considerable progress was made over the last few years in understanding the mechanism of folding of cytochrome c(551), a small acidic hemeprotein from Pseudomonas aeruginosa. Comparison of our results with those obtained by others on horse heart cytochrome c allows to draw some general conclusions on the structural features that are common determinants in the folding of members of the cytochrome c family.

Cytochrome c551 as a model system for protein folding / Brunori, Maurizio; Bigotti, Maria Giulia; Cutruzzola', Francesca; Gianni, Stefano; TRAVAGLINI ALLOCATELLI, Carlo. - In: BIOPHYSICAL CHEMISTRY. - ISSN 0301-4622. - 100(2003), pp. 409-419. [10.1016/S0301-4622(02)00295-8]

Cytochrome c551 as a model system for protein folding

BRUNORI, Maurizio;BIGOTTI, Maria Giulia;CUTRUZZOLA', Francesca;GIANNI, STEFANO;TRAVAGLINI ALLOCATELLI, Carlo
2003

Abstract

Considerable progress was made over the last few years in understanding the mechanism of folding of cytochrome c(551), a small acidic hemeprotein from Pseudomonas aeruginosa. Comparison of our results with those obtained by others on horse heart cytochrome c allows to draw some general conclusions on the structural features that are common determinants in the folding of members of the cytochrome c family.
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/11573/364932
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