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.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
