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Results: 1-11 |
Results: 11
Comparison of the creep properties of single crystal and polycrystalline diamond cutting tool materials
Authors: Harris, TK Brookes, EJ Daniel, R
Citation: Tk. Harris et al., Comparison of the creep properties of single crystal and polycrystalline diamond cutting tool materials, DIAM RELAT, 10(3-7), 2001, pp. 755-759
The structural basis for the perturbed pK(a) of the catalytic base in 4-oxalocrotonate tautomerase: Kinetic and structural effects of mutations of Phe-50
Authors: Czerwinski, RM Harris, TK Massiah, MA Mildvan, AS Whitman, CP
Citation: Rm. Czerwinski et al., The structural basis for the perturbed pK(a) of the catalytic base in 4-oxalocrotonate tautomerase: Kinetic and structural effects of mutations of Phe-50, BIOCHEM, 40(7), 2001, pp. 1984-1995
Mechanistic implications of methylglyoxal synthase complexed with phosphoglycolohydroxamic acid as observed by X-ray crystallography and NMR spectroscopy
Authors: Marks, GT Harris, TK Massiah, MA Mildvan, AS Harrison, DHT
Citation: Gt. Marks et al., Mechanistic implications of methylglyoxal synthase complexed with phosphoglycolohydroxamic acid as observed by X-ray crystallography and NMR spectroscopy, BIOCHEM, 40(23), 2001, pp. 6805-6818
NMR studies of strong hydrogen bonds in enzymes and in a model compound
Authors: Harris, TK Zhao, Q Mildvan, AS
Citation: Tk. Harris et al., NMR studies of strong hydrogen bonds in enzymes and in a model compound, J MOL STRUC, 552, 2000, pp. 97-109
Mutational, kinetic, and NMR studies of the roles of conserved glutamate residues and of lysine-39 in the mechanism of the MutT pyrophosphohydrolase
Authors: Harris, TK Wu, G Massiah, MA Mildvan, AS
Citation: Tk. Harris et al., Mutational, kinetic, and NMR studies of the roles of conserved glutamate residues and of lysine-39 in the mechanism of the MutT pyrophosphohydrolase, BIOCHEM, 39(7), 2000, pp. 1655-1674
NMR evidence for a short, strong hydrogen bond at the active site of a cholinesterase
Authors: Viragh, C Harris, TK Reddy, PM Massiah, MA Mildvan, AS Kovach, IM
Citation: C. Viragh et al., NMR evidence for a short, strong hydrogen bond at the active site of a cholinesterase, BIOCHEM, 39(51), 2000, pp. 16200-16205
High-precision measurement of hydrogen bond lengths in proteins by nuclearmagnetic resonance methods
Authors: Harris, TK Mildvan, AS
Citation: Tk. Harris et As. Mildvan, High-precision measurement of hydrogen bond lengths in proteins by nuclearmagnetic resonance methods, PROTEINS, 35(3), 1999, pp. 275-282
Nuclear magnetic resonance methods for the detection and study of low-barrier hydrogen bonds on enzymes
Authors: Mildvan, AS Harris, TK Abeygunawardana, C
Citation: As. Mildvan et al., Nuclear magnetic resonance methods for the detection and study of low-barrier hydrogen bonds on enzymes, METH ENZYM, 308, 1999, pp. 219-245
Kinetic, stereochemical, and structural effects of mutations of the activesite arginine residues in 4-oxalocrotonate tautomerase
Authors: Harris, TK Czerwinski, RM Johnson, WH Legler, PM Abeygunawardana, C Massiah, MA Stivers, JT Whitman, CP Mildvan, AS
Citation: Tk. Harris et al., Kinetic, stereochemical, and structural effects of mutations of the activesite arginine residues in 4-oxalocrotonate tautomerase, BIOCHEM, 38(38), 1999, pp. 12343-12357
Effects of mutations of the active site arginine residues in 4-oxalocrotonate tautomerase on the pK(a) values of active site residues and on the pH dependence of catalysis
Authors: Czerwinski, RM Harris, TK Johnson, WH Legler, PM Stivers, JT Mildvan, AS Whitman, CP
Citation: Rm. Czerwinski et al., Effects of mutations of the active site arginine residues in 4-oxalocrotonate tautomerase on the pK(a) values of active site residues and on the pH dependence of catalysis, BIOCHEM, 38(38), 1999, pp. 12358-12366
Proton transfer in the mechanism of triosephosphate isomerase
Authors: Harris, TK Cole, RN Comer, FI Mildvan, AS
Citation: Tk. Harris et al., Proton transfer in the mechanism of triosephosphate isomerase, BIOCHEM, 37(47), 1998, pp. 16828-16838
Risultati: 1-11 |