title: Population and structure determination of hidden folding intermediates by native-state hydrogen exchange-directed protein engineering and nuclear magnetic resonance.
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.
authors.affiliation: Laboratory of Biochemistry, National Cancer Institute, National Institues of Health, Bethesda, MD, USA.
authors.forename: Yawen
authors.initials: Y
authors.lastname: Bai
authors.forename: Hanqiao
authors.initials: H
authors.lastname: Feng
authors.forename: Zheng
authors.initials: Z
authors.lastname: Zhou
mesh_terms: D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011487:Protein Conformation; D015202:Protein Engineering / Q000379:methods*; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*
chemical_list: D011506:Proteins