Nomenclature for the applications of nuclear magnetic resonance to the study of enzymes

Abragam, 1973 Bachovchin, 2001, Contributions of NMR spectroscopy to the study of hydrogen bonds in serine protease active sites, Magn. Reson. Chem., 39, S199, 10.1002/mrc.951 Balazs, 2013, Identifying critical unrecognized sugar-protein interactions in G10 xylanases from Geobacillus stearothermophilus using STD NMR, FEBS J, 280, 4652, 10.1111/febs.12437 Becker, 1980 Berliner, 1976 Berliner, 1989, Laser chemically induced dynamic nuclear polarization studies in proteins: α-lactalbumin, Arch. Biol. Med. Exp., 22, 123 Bhunia, 2012, Applications of saturation transfer difference NMR in biological systems, Drug Discov. Today, 17, 505, 10.1016/j.drudis.2011.12.016 Billiter, 1989, Comparison of the high-resolution structures of the α-amylase inhibitor tendamistat determined by nuclear magnetic resonance in solution and by X-ray diffraction in single crystals, J. Mol. Biol., 206, 677, 10.1016/0022-2836(89)90575-5 Bloch, 1946, Nuclear induction, Phys. Rev., 70, 460, 10.1103/PhysRev.70.460 Bloembergen, 1957, Proton relaxation times in paramagnetic solutions, J. Chem. Phys., 27, 572, 10.1063/1.1743771 Blume, 2009, Specificity of ligand binding to yeast hexokinase PII studied by STD-NMR, Carbohydr Res, 344, 1567, 10.1016/j.carres.2009.01.002 Cambell, 1993, The two-dimensional transferred nuclear Overhauser effect. Theory and practice, Annu. Rev. Biophys. Biomol. Struct., 22, 99, 10.1146/annurev.bb.22.060193.000531 Cleland, 1979, Chromium (III) and cobalt (II) nucleotides as biological probes, Adv. Inorg. Bichem, 1, 163 Clore, 2011, Exploring sparsely populated states of macromolecules by diamagnetic and paramagnetic NMR relaxation, Prot. Sci., 20, 229, 10.1002/pro.576 Clore, 1984, Structure of the ribotrinucleoside diphosphate codon UpUpC bound to tRNAphe from yeast. A time-dependent transferred nuclear Overhauser enhancement study, J. Mol. Biol., 174, 163, 10.1016/0022-2836(84)90370-X Danielson, 1996, Use of 19F NMR to probe protein structure and conformational changes, Annu. Rev. Biophys. Biomol. Struct., 25, 163, 10.1146/annurev.bb.25.060196.001115 Donaldson, 2001, Structural characterization of proteins with an attached ATCUN motif by paramagnetic relaxation enhancement NMR spectroscopy, J. Am. Chem. Soc., 123, 9843, 10.1021/ja011241p Dwek, 1973 Ernst, 1987 Geric, 1981, Fluorine magnetic resonance in biochemistry, vol I, 139 Henzler-Wildman, 2007, Dynamic personalities of proteins, Nature, 450, 964, 10.1038/nature06522 Henzler-Wildman, 2007, Intrinsic motions along an enzymatic reaction trajectory, Nature, 450, 838, 10.1038/nature06410 Hunkapiller, 1973, Carbon nuclear magnetic resonance studies of the histidine residue in (alpha) lytic protease. Implications for the catalytic mechanism of serine proteases, Biochemistry, 12, 4732, 10.1021/bi00747a028 James, 1974, The role of the lysine residue at the active site of creatine kinase, J. Biol. Chem., 249, 2599, 10.1016/S0021-9258(19)42773-7 James, 1975 Kaptein, 1982, Photo-CIDNP studies, vol 4, 145 Kevin, 1998, The use of 2H, 13C, 15N multidimensional NMR to study the structure and dynamics of proteins, Annu. Rev. Biophys. Biomol. Struct., 27, 357, 10.1146/annurev.biophys.27.1.357 Koide, 1989, Conformation of NAD+ bound to allosteric l-lactate dehydrogenase activated by chemical modification, J. Biol. Chem., 264, 8676, 10.1016/S0021-9258(18)81845-2 Kuntothom, 2010, Binding of β-D-glucosides and β-D-mannosides by rice and barley β-d-glycosidases with distinct substrate specificities, Biochemistry, 49, 8779, 10.1021/bi101112c Leanz, 1986, Kinetic and nuclear magnetic resonance study of the interaction of NADP+ and NADH with chicken liver fatty acid synthase, Biochemistry, 25, 5617, 10.1021/bi00367a041 Live, 1987, Binding of oxytocin and 8-arginine–vasopressin to neurophysin studied by 1N-NMR using magnetization transfer and indirect detection via protons, Biochemistry, 16, 5 Lucas, 2003, Transferred nuclear Overhauser effect in nuclear magnetic resonance diffusion measurements of ligand–protein binding, Anal. Chem., 75, 627, 10.1021/ac020563o Malthouse, 1986, 13C NMR of enzymes, Prog. Nucl. Magn. Reson. Spectrosc., 18, 1, 10.1016/0079-6565(85)80002-9 Markley, 1975, Observation of histidine residues in proteins by means of nuclear magnetic resonance spectroscopy, Acc. Chem. Res., 8, 70, 10.1021/ar50086a004 Mayer, 1999, Characterization of ligand binding by saturation transfer difference NMR spectroscopy, Angew. Chem. Int. Ed, 44, 4172 Meadows, 1986, Nuclear magnetic resonance studies of the structure and binding sites of enzymes IV. Cytidine 3′-monophosphate binding to ribonuclease, Proc. Natl. Acad. Sci. USA, 61, 406, 10.1073/pnas.61.2.406 Meshitsuka, 1981, Proton NMR studies of the histidine residues of rabbit muscle pyruvate kinase and of its phosphoenolpyruvate complex, J. Biol. Chem., 256, 4460, 10.1016/S0021-9258(19)69457-3 Meyer, 1988, Analysis of an enzyme-substrate complex by X-ray crystallography and transferred nuclear Overhauser enhancement measurements: porcine pancreatic elastase and hexapeptide, Biochemistry, 27, 125, 10.1021/bi00402a035 Mildvan, 1967, Kinetic and magnetic resonance studies of pyruvate kinase. III. The enzyme–metal–phosphoryl bridge complex in the fluorokinase reaction, Biochemistry, 6, 1805, 10.1021/bi00858a032 Mildvan, 1989, NMR studies of the interactions of substrates with enzymes and their peptide fragments, FASEB J., 3, 1705, 10.1096/fasebj.3.6.2649401 Milon, 1990, Transferred nuclear Overhauser effect analysis of membrane-bound enkephalin analogs by 1H nuclear magnetic resonance: correlation between activities and membrane-bound conformations, Biochemistry, 29, 65, 10.1021/bi00453a009 Monasterio, 1987, I9F Nuclear magnetic resonance measurement of the distance between the E-site GTP and the high-affinity Mg2+ in tubulin, Biochemistry, 26, 6099, 10.1021/bi00393a023 Monasterio, 1987, lnhibition of tubulin self-assembly and tubulin–colchicine GTPase activity by guanosine 5′-(γ-fluorotriphosphate), Biochemistry, 26, 6091, 10.1021/bi00393a022 Monasterio, 1995, Tubulin–tyrosine ligase catalyzes covalent binding of m-fluorotyrosine to tubulin. Kinetic and 19F-NMR Studies, FEBS Lett., 374, 165, 10.1016/0014-5793(95)01099-Z Monasterio, 2001, Rate constants determined by nuclear magnetic resonance, Methods, 24, 97, 10.1006/meth.2001.1171 Orengo, 1994, Classification of protein folds, Curr. Opin. Struct. Biol., 4, 429, 10.1016/S0959-440X(94)90113-9 Redfield, 1989, Use of 13C and 15N isotope labels for proton nuclear magnetic resonance and nuclear Overhauser effect. Structural and dynamic studies of larger proteins and nucleic acids, Arch. Biol. Med. Exp., 22, 129 Roberts, 1970, Nuclear magnetic resonance spectroscopy of amino acids, peptides, and proteins, Adv. Prot. Chem., 24, 447, 10.1016/S0065-3233(08)60246-6 Solomon, 1955, Relaxation processes in a system of two spins, Phys. Rev., 99, 559, 10.1103/PhysRev.99.559 Sykes, 1980, Biosynthesis and 19F NMR characterization of fluoroamino acid containing proteins, vol I, 1 Tugarinov, 2004, Nuclear magnetic resonance spectroscopy of high-molecular weight proteins, Annu. Rev. Biochem., 73, 107, 10.1146/annurev.biochem.73.011303.074004 Wüthrich, 1986