Article
Effects of heme on the structure of the denatured state and folding kinetics of cytochrome b562.
Journal of molecular biology - 11 Feb 2005
Garcia Pascal, Bruix Marta, Rico Manuel, Ciofi-Baffoni Simone, Banci Lucia, Ramachandra Shastry M C, Roder Heinrich, de Lumley Woodyear Thierry, Johnson Christopher M, Fersht Alan R, Barker Paul D
Abstract excerpt
Heme-linked proteins, such as cytochromes, are popular subjects for protein folding studies. There is the underlying question of whether the heme affects the structure of the denatured state by cross-linking it and forming other interactions, which would perturb the folding pathway. We have studied wild-type and mutant cytochrome b562 from Escherichia coli, a 106 residue four-alpha-helical bundle. The holo...
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.