Cytochrome c(551) as a model system for protein folding.
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.
Brunori
Maurizio
M
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
Bigotti
Maria Giulia
MG
Cutruzzolà
Francesca
F
Gianni
Stefano
S
Travaglini-Allocatelli
Carlo
C
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
D001426:Bacterial Proteins; D003574:Cytochrome c Group; D014508:Urea; C017167:cytochrome C(551); D019791:Guanidine