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Structural Characterization of a Partly Folded Apomyoglobin Intermediate

Hughson, Frederick M., Wright, Peter E., Baldwin, Robert L.·1990·Science

Abstract

To understand why proteins adopt particular three-dimensional structures, it is important to elucidate the hierarchy of interactions that stabilize the native state. Proteins in partly folded states can be used to dissect protein organizational hierarchies. A partly folded apomyoglobin intermediate has now been characterized structurally by trapping slowly exchanging peptide NH protons and analyzing them by two-dimensional 1 H-NMR (nuclear magnetic resonance). Protons in the A, G, and H helix regions are protected from exchange, while protons in the B and E helix regions exchange freely. On the basis of these results and the three-dimensional structure of native myoglobin, a structural model is presented for the partly folded intermediate in which a compact subdomain retains structure while the remainder of the protein is essentially unfolded.

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Metadata

Authors
Hughson, F. M., Wright, P. E., & Baldwin, R. L.
Venue
Science
Published
1990-09-28
Volume
249
Issue
4976
Pages
1544-1548
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W1975495422
Cited by
705
References
0
FWCI
13.78
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Structural Characterization of a Partly Folded Apomyoglobin Intermediate. https://app.cochat.ai/papers/10.1126/science.2218495
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Hughson, F. M., Wright, P. E., & Baldwin, R. L. (1990). Structural Characterization of a Partly Folded Apomyoglobin Intermediate. Science. https://doi.org/10.1126/science.2218495

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