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 μis time scale. We show that the early folding kinetics of apomyoglobin may be understood as the associati...
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Veröffentlicht in: | Protein science 1998-02, Vol.7 (2), p.480-490 |
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Hauptverfasser: | , |
Format: | Artikel |
Sprache: | eng |
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Online-Zugang: | Volltext |
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Zusammenfassung: | 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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ISSN: | 0961-8368 1469-896X |
DOI: | 10.1002/pro.5560070229 |