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Science 28 September 1990:
Vol. 249. no. 4976, pp. 1544 - 1548
DOI: 10.1126/science.2218495
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Articles

Science, Vol 249, Issue 4976, 1544-1548
Copyright © 1990 by American Association for the Advancement of Science

articles

Structural characterization of a partly folded apomyoglobin intermediate

FM Hughson, PE Wright, and RL Baldwin

Department of Biochemistry, Beckman Center, Stanford University School of Medicine, CA 94305.

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 1H-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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