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...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Protein science 1998-02, Vol.7 (2), p.480-490
Hauptverfasser: Pappu, Rohit V., Weaver, David L.
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
Beschreibung
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.
ISSN:0961-8368
1469-896X
DOI:10.1002/pro.5560070229