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- Currently displaying 22141 - 22160 of 29684 publications
Protein Folding Kinetics from Magnetization Transfer Nuclear Magnetic Resonance
Biochemistry
(2002)
23
4267
(doi: 10.1021/bi00314a001)
High-Resolution Nitrogen-15 Nuclear Magnetic Resonance Studies of α-Lytic Protease in Solid State. Direct Comparison of Enzyme Structure in Solution and in the Solid State
Biochemistry
(2002)
23
5933
(doi: 10.1021/bi00320a007)
Formaldehyde Metabolism by Escherichia coli. Carbon and Solvent Deuterium Incorporation into Glycerol, 1,2-Propanediol, and 1,3-Propanediol
Biochemistry
(2002)
24
4148
(doi: 10.1021/bi00336a050)
Conformations of two duplex forms of d(TCGA) in slow-exchange equilibrium characterized by NMR
Biochemistry
(2002)
24
4325
(doi: 10.1021/bi00337a011)
Probing histidine-substrate interactions in tyrosyl-tRNA synthetase using asparagine and glutamine replacements.
Biochemistry
(2002)
24
5106
(doi: 10.1021/bi00340a022)
Reversible dissociation of dimeric tyrosyl-tRNA synthetase by mutagenesis at the subunit interface.
Biochemistry
(2002)
24
5852
(doi: 10.1021/bi00342a024)
Fine structure-activity analysis of mutations at position 51 of tyrosyl-tRNA synthetase.
Biochemistry
(2002)
24
5858
(doi: 10.1021/bi00342a025)
Use of binding energy in catalysis analyzed by mutagenesis of the tyrosyl-tRNA synthetase
Biochemistry
(2002)
25
1881
(doi: 10.1021/bi00356a007)
Natural variation of tyrosyl-tRNA synthetase and comparison with engineered mutants.
Biochemistry
(2002)
25
1887
(doi: 10.1021/bi00356a008)
INTERNAL THERMODYNAMICS OF POSITION 51 MUTANTS AND NATURAL VARIANTS OF TYROSYL-TRANSFER RNA-SYNTHETASE
Biochemistry
(2002)
25
1891
(doi: 10.1021/bi00356a009)
Formaldehyde metabolism by Escherichia coli. Detection by in vivo 13C NMR spectroscopy of S-(hydroxymethyl)glutathione as a transient intracellular intermediate.
Biochemistry
(2002)
25
4504
(doi: 10.1021/bi00364a008)
Free energy of hydrolysis of tyrosyl adenylate and its binding to wild-type and engineered mutant tyrosyl-tRNA synthetases
Biochemistry
(2002)
25
6603
(doi: 10.1021/bi00369a040)
The valyl-tRNA synthetase from Bacillus stearothermophilus has considerable sequence homology with the isoleucyl-tRNA synthetase from Escherichia coli
Biochemistry
(2002)
26
2480
(doi: 10.1021/bi00383a012)
Effects of engineering complementary charged residues into the hydrophobic subunit interface of tyrosyl-tRNA synthetase
Biochemistry
(2002)
26
4131
(doi: 10.1021/bi00387a058)
Site-directed mutagenesis in the effector site of Escherichia coli phosphofructokinase
Biochemistry
(2002)
26
4143
(doi: 10.1021/bi00387a060)
Structure-activity relationships in engineered proteins: analysis of use of binding energy by linear free energy relationships.
Biochemistry
(2002)
26
6030
(doi: 10.1021/bi00393a013)
Structure-activity relationships in engineered proteins: characterization of disruptive deletions in the .alpha.-ammonium group binding site of tyrosyl-tRNA synthetase
Biochemistry
(2002)
26
6038
(doi: 10.1021/bi00393a014)
Site-directed mutagenesis reveals transition-state stabilization as a general catalytic mechanism for aminoacyl-tRNA synthetases.
Biochemistry
(2002)
26
7246
(doi: 10.1021/bi00397a008)
Dissection of the structure and activity of the tyrosyl-tRNA synthetase by site-directed mutagenesis.
Biochemistry
(2002)
26
8031
(doi: 10.1021/bi00399a001)
