Abstract:
:The structures of the major folding intermediate, the transition state for folding, and the folded state of barnase have been previously characterized. We now add a further step toward a complete picture of the folding of barnase by reporting the backbone 15N, 13C, and 1H NMR assignments for barnase unfolded at pH 1.8 and 30 degrees C. These assignments, which were obtained from a combination of heteronuclear magnetization transfer and backbone triple-resonance NMR experiments, constitute the first stage in the structural characterization of this denatured state by NMR. Interresidue nuclear Overhauser effect contacts and deviations from 1H random-coil chemical shifts provide evidence for stable residual structure. The structured regions span residues in the native protein that contain its major alpha-helix and central strands of the beta-sheet. Earlier experiments have shown that these regions are predominantly intact in the major folding intermediate and that their docking is partly rate determining in folding.
journal_name
Proc Natl Acad Sci U S Aauthors
Arcus VL,Vuilleumier S,Freund SM,Bycroft M,Fersht ARdoi
10.1073/pnas.91.20.9412subject
Has Abstractpub_date
1994-09-27 00:00:00pages
9412-6issue
20eissn
0027-8424issn
1091-6490journal_volume
91pub_type
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journal_title:Proceedings of the National Academy of Sciences of the United States of America
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