title: Indirect use of deuterium in solution NMR studies of protein structure and hydrogen bonding.
abstract: A description of the utility of deuteration in protein NMR is provided with an emphasis on quantitative evaluation of the effects of deuteration on a number of NMR parameters of proteins: (1) chemical shifts, (2) scalar coupling constants, (3) relaxation properties (R1 and R2 rates) of nuclei directly attached to one or more deuterons as well as protons of methyl groups in a highly deuterated environment, (4) scalar relaxation of 15N and 13C nuclei in 15N-D and 13C-D spin systems as a measure of hydrogen bonding strength, and (5) NOE-based applications of deuteration in NMR studies of protein structure. The discussion is restricted to the 'indirect' use of deuterium in the sense that the description of NMR parameters and properties of the nuclei affected by nearby deuterons (15N, 13C, 1H) is provided rather than those of deuterium itself.
authors.affiliation: Department of Chemistry and Biochemistry, University of Maryland, College Park, MD 20742, United States. Electronic address: vitali@umd.edu.
authors.forename: Vitali
authors.initials: V
authors.lastname: Tugarinov
mesh_terms: D003903:Deuterium / Q000737:chemistry*; D006860:Hydrogen Bonding; D019906:Nuclear Magnetic Resonance, Biomolecular; D011506:Proteins / Q000737:chemistry*; D012996:Solutions
chemical_list: D011506:Proteins; D012996:Solutions; D003903:Deuterium
keywords: BIRD; CPMG; CSA; Carr–Purcell–Meiboom–Gill pulse train; Deuteration; Deuterium isotope shifts; Hydrogen bonds; MSG; Malate Synthase G; NOE; Protein backbone geometry; Protein dynamics; QCC; RDC; Spin relaxation in deuterium-containing spin-systems; TROSY; bilinear rotation decoupling; chemical shift anisotropy; nuclear Overhauser effect; quadrupolar coupling constant; residual dipolar coupling; transverse relaxation optimized spectroscopy