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Updated: Jul 20, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
Published on: September 17, 2017
Population and structure determination of hidden folding intermediates by native-state hydrogen exchange-directed
Yawen Bai1, Hanqiao Feng, Zheng Zhou
1Laboratory of Biochemistry, National Cancer Institute, National Institues of Health, Bethesda, MD, USA.
Abstract:
Structural characterization of folding intermediates has been one of the important steps toward understanding the mechanism of protein folding. However, it has been very difficult to obtain high-resolution structures of folding intermediates. Such results have become available only very recently. Here, we review a procedure that uses the native-state amide hydrogen exchange-directed protein engineering method to populate partially unfolded intermediates and multidimensional NMR to solve the high-resolution structures of the intermediates.
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