| Literature DB >> 12646380 |
Maurizio Brunori1, Maria Giulia Bigotti, Francesca Cutruzzolà, Stefano Gianni, Carlo Travaglini-Allocatelli.
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.Entities:
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Year: 2003 PMID： 12646380 DOI： 10.1016/s0301-4622(02)00295-8
Source DB: PubMed Journal: Biophys Chem ISSN： 0301-4622 Impact factor: 2.352