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Formation of a Molten Globule Intermediate Early in the Kinetic Folding Pathway of Apomyoglobin

Jennings, Patricia A., Wright, Peter E.·1993·Science

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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Metadata

Authors
Jennings, P. A., & Wright, P. E.
Venue
Science
Published
1993-11-05
Volume
262
Issue
5135
Pages
892-896
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2074991560
Cited by
728
References
0
FWCI
13.11
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Formation of a Molten Globule Intermediate Early in the Kinetic Folding Pathway of Apomyoglobin. https://app.cochat.ai/papers/10.1126/science.8235610
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Jennings, P. A., & Wright, P. E. (1993). Formation of a Molten Globule Intermediate Early in the Kinetic Folding Pathway of Apomyoglobin. Science. https://doi.org/10.1126/science.8235610

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Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.