A funneled energy landscape for cytochrome c directly predicts the sequential folding route inferred from hydrogen exchange experiments.
Proteins fold through a variety of mechanisms. For a given protein, folding routes largely depend on the protein's stability and its native-state geometry, because the landscape is funneled. These ideas are corroborated for cytochrome c by using a coarse-grained topology-based model with a perfect funnel landscape that includes explicit modeling of the heme. The results show the importance of the heme as a nucleation site and explain the observed hydrogen exchange patterns of cytochrome c within the context of energy landscape theory.
Weinkam
Patrick
P
Center for Theoretical Biological Physics and Department of Physics, University of California at San Diego, La Jolla, CA 92093, USA.
Zong
Chenghang
C
Wolynes
Peter G
PG
D055592:Biophysical Phenomena; D001703:Biophysics; D045304:Cytochromes c / Q000737:chemistry*; D006418:Heme / Q000737:chemistry; D006859:Hydrogen / Q000737:chemistry; D008958:Models, Molecular; D011487:Protein Conformation; D017510:Protein Folding; D013816:Thermodynamics
D006418:Heme; D006859:Hydrogen; D045304:Cytochromes c