Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin.

Abstract

Hydrogen exchange pulse labeling and stopped-flow circular dichroism were used to establish that the structure of the earliest detectable intermediate formed during refolding of apomyoglobin corresponds closely to that of a previously characterized equilibrium molten globule. This compact, cooperatively folded intermediate was formed in less than 5 milliseconds and contained stable, hydrogen-bonded secondary structure localized in the A, G, and H helices and part of the B helix. The remainder of the B helix folded on a much slower time scale, followed by the C and E helices and the CD loop. The data indicate that a molten globule intermediate was formed on the kinetic folding pathway.

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@article{Jennings1993FormationOA, title={Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin.}, author={Patricia Ann Jennings and Peter E. Wright}, journal={Science}, year={1993}, volume={262 5135}, pages={892-6} }