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Title: Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin. Author: Jennings PA, Wright PE. Journal: Science; 1993 Nov 05; 262(5135):892-6. PubMed ID: 8235610. 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.[Abstract] [Full Text] [Related] [New Search]