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Science 5 November 1993:
Vol. 262. no. 5135, pp. 892 - 896
DOI: 10.1126/science.8235610
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Articles

Science, Vol 262, Issue 5135, 892-896
Copyright © 1993 by American Association for the Advancement of Science

articles

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

PA Jennings and PE Wright

Department of Molecular Biology, Scripps Research Institute, La Jolla, California 92037.

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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