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Protein Science, Vol 7, Issue 2 480-490, Copyright © 1998 by Cold Spring Harbor Laboratory Press

ARTICLE

The early folding kinetics of apomyoglobin

R. V. PAPPU and D. L. WEAVER
Department of Biochemistry & Molecular Biophysics, Washington University School of Medicine, St. Louis, Missouri 63110 Molecular Modeling Laboratory, Department of Physics, Tufts University, Medford, Massachusetts 02155

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 {mu}s 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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