Solid state NMR: new tools for insight into enzyme function.
NMR has had considerable impact in enzymology, probing evidence for ionization states, conformational 'strain', compressed interactions, electronically unusual species, and conformational dynamics of enzymes. Solid-state NMR is becoming increasingly important in studying enzymes because of a number of recent tools for analysis of proteins by SSNMR, and because of the growing ability to isolate the species of interest for analysis. Here, we review recent studies of a Michaelis complex, of the dynamic functioning of membrane-associated enzymes, and initial studies of several enzymes with redox-active and paramagnetic centers.
McDermott
Ann
A
Columbia University, Department of Chemistry, New York, NY 10027, United States. aem5@columbia.edu
Polenova
Tatyana
T
D004578:Electron Spin Resonance Spectroscopy / Q000379:methods; D004798:Enzymes / Q000737:chemistry* / Q000378:metabolism*; D045726:Metalloproteases / Q000737:chemistry / Q000378:metabolism; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D010084:Oxidation-Reduction; D011487:Protein Conformation; D013816:Thermodynamics
D004798:Enzymes; D045726:Metalloproteases