The early folding kinetics of apomyoglobin.
The folding pathway of apomyoglobin has been experimentally shown to have early kinetic intermediates involving the A, B, G, and H helices. The earliest detected kinetic events occur on a ns to micros time scale. We show that the early folding kinetics of apomyoglobin may be understood as the association of nascent helices through a network of diffusion-collision-coalescence steps G + H <--> GH + A <--> AGH + B <--> ABGH obtained by solving the diffusion-collision model in a chemical kinetics approximation. Our reproduction of the experimental results indicates that the model is a useful way to analyze folding data. One prediction from our fit is that the nascent A and H helices should be relatively more helix-like before coalescence than the other apomyoglobin helices.
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Department of Biochemistry & Molecular Biophysics, Washington University School of Medicine, St. Louis, Missouri 63110, USA.
Weaver
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D001059:Apoproteins / Q000737:chemistry*; D004058:Diffusion; D007700:Kinetics; D008956:Models, Chemical; D009211:Myoglobin / Q000737:chemistry*; D017510:Protein Folding
D001059:Apoproteins; D009211:Myoglobin; C010857:apomyoglobin