Brunori Maurizio, Bigotti Maria Giulia, Cutruzzolà Francesca, Gianni Stefano, Travaglini-Allocatelli Carlo
Istituto Pasteur-Fondazione Cenci Bolognetti, Department of Biochemical Sciences, Università di Roma La Sapienza, P. le A. Moro 5, 00185 Roma, Italy.
Biophys Chem. 2003;100(1-3):409-19. doi: 10.1016/s0301-4622(02)00295-8.
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.
