title: Cytochrome c(551) as a model system for protein folding.
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.
authors.affiliation: Istituto Pasteur-Fondazione Cenci Bolognetti, Department of Biochemical Sciences, Università di Roma La Sapienza, P. le A. Moro 5, 00185 Roma, Italy. maurizio.brunori@uniroma1.it
authors.forename: Maurizio
authors.initials: M
authors.lastname: Brunori
authors.forename: Maria Giulia
authors.initials: MG
authors.lastname: Bigotti
authors.forename: Francesca
authors.initials: F
authors.lastname: Cutruzzolà
authors.forename: Stefano
authors.initials: S
authors.lastname: Gianni
authors.forename: Carlo
authors.initials: C
authors.lastname: Travaglini-Allocatelli
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics; D003574:Cytochrome c Group / Q000737:chemistry* / Q000235:genetics; D019791:Guanidine / Q000737:chemistry; D007700:Kinetics; D008956:Models, Chemical; D009154:Mutation / Q000235:genetics; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding; D011550:Pseudomonas aeruginosa / Q000201:enzymology; D014508:Urea / Q000737:chemistry
chemical_list: D001426:Bacterial Proteins; D003574:Cytochrome c Group; D014508:Urea; C017167:cytochrome C(551); D019791:Guanidine