title: Solid state NMR: new tools for insight into enzyme function.
abstract: 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.
authors.affiliation: Columbia University, Department of Chemistry, New York, NY 10027, United States. aem5@columbia.edu
authors.forename: Ann
authors.initials: A
authors.lastname: McDermott
authors.forename: Tatyana
authors.initials: T
authors.lastname: Polenova
mesh_terms: 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
chemical_list: D004798:Enzymes; D045726:Metalloproteases