Monitoring protein folding at atomic resolution.
Elucidation of the mechanisms by which proteins fold from disordered conformations to their unique native conformations is one of the most challenging tasks facing structural biologists. Understanding the mechanism(s) of protein folding involves the characterization of all structural species that occur in the protein-folding reaction. Nuclear magnetic resonance (NMR) spectroscopy is a powerful and versatile technique that provides an avenue to investigate the structures of the various conformational states at the residue level along the protein-folding reaction coordinate. In this Account, we provide a comprehensive review of the recent progress on the applications of NMR to monitor equilibrium and kinetic conformational states of the protein-folding reaction.
Kumar
Thallapuranam Krishnaswamy S
TK
Department of Chemistry and Biochemistry, University of Arkansas, Fayetteville, AR 72701, USA.
Yu
Chin
C
D001059:Apoproteins / Q000737:chemistry / Q000378:metabolism; D016220:Fibroblast Growth Factor 1 / Q000737:chemistry / Q000378:metabolism; D006859:Hydrogen / Q000737:chemistry; D007700:Kinetics; D009211:Myoglobin / Q000737:chemistry / Q000378:metabolism; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*
D001059:Apoproteins; D009211:Myoglobin; D011506:Proteins; C010857:apomyoglobin; D016220:Fibroblast Growth Factor 1; D006859:Hydrogen