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.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Bacterial Proteins / chemistry*
-
Bacterial Proteins / genetics
-
Cytochrome c Group / chemistry*
-
Cytochrome c Group / genetics
-
Guanidine / chemistry
-
Kinetics
-
Models, Chemical
-
Mutation / genetics
-
Protein Conformation
-
Protein Denaturation
-
Protein Folding*
-
Pseudomonas aeruginosa / enzymology
-
Urea / chemistry
Substances
-
Bacterial Proteins
-
Cytochrome c Group
-
Urea
-
cytochrome C(551)
-
Guanidine