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The early folding kinetics of apomyoglobin
Author(s) -
Pappu Rohit V.,
Weaver David L.
Publication year - 1998
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.5560070229
Subject(s) - kinetics , coalescence (physics) , chemistry , folding (dsp implementation) , kinetic energy , protein folding , crystallography , helix (gastropod) , biophysics , physics , biochemistry , biology , ecology , astrobiology , snail , electrical engineering , engineering , quantum mechanics
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 μis time scale. We show that the early folding kinetics of apomyoglobin may be understood as the association of nascent helices through a network of diffusioncollision‐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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