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- Currently displaying 22341 - 22360 of 29682 publications
Assignment of histidine resonances in the proton NMR (500 MHz) spectrum of subtilisin BPN' using site-directed mutagenesis
Biochemistry
(2002)
27
7390
(doi: 10.1021/bi00419a033)
Establishing the misacylation/deacylation of the tRNA pathway for the editing mechanism of prokaryotic and eukaryotic valyl-tRNA synthetases.
Biochemistry
(2002)
18
1238
(doi: 10.1021/bi00574a019)
Cysteinyl-tRNA synthetase from Escherichia coli does not need an editing mechanism to reject serine and alanine. High binding energy of small groups in specific molecular interactions.
Biochemistry
(2002)
18
1245
(doi: 10.1021/bi00574a020)
Reconstruction by site-directed mutagenesis of the transition state for the activation of tyrosine by the tyrosyl-tRNA synthetase: a mobile loop envelopes the transition state in an induced-fit mechanism
Biochemistry
(2002)
27
1581
(doi: 10.1021/bi00405a028)
Relationships between apparent binding energies measured in site-directed mutagenesis experiments and energetics of binding and catalysis.
Biochemistry
(2002)
27
1577
(doi: 10.1021/bi00405a027)
Sequential1H NMR Assignments and Secondary Structure of Hen Egg White Lysozyme in Solution
Biochemistry
(2002)
27
122
(doi: 10.1021/bi00401a020)
Investigation of transition-state stabilization by residues histidine-45 and threonine-40 in the tyrosyl-tRNA synthetase
Biochemistry
(2002)
26
8524
(doi: 10.1021/bi00400a005)
Dissection of the structure and activity of the tyrosyl-tRNA synthetase by site-directed mutagenesis.
Biochemistry
(2002)
26
8031
(doi: 10.1021/bi00399a001)
Site-directed mutagenesis reveals transition-state stabilization as a general catalytic mechanism for aminoacyl-tRNA synthetases
Biochemistry
(2002)
26
7246
(doi: 10.1021/bi00397a008)
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)
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)
Site-directed mutagenesis in the effector site of Escherichia coli phosphofructokinase.
Biochemistry
(2002)
26
4143
(doi: 10.1021/bi00387a060)
An editing mechanism for the methionyl-tRNA synthetase in the selection of amino acids in protein synthesis.
Biochemistry
(2002)
18
1250
(doi: 10.1021/bi00574a021)
Evidence for the double-sieve editing mechanism in protein synthesis. Steric exclusion of isoleucine by valyl-tRNA synthetases
Biochemistry
(2002)
18
2627
(doi: 10.1021/bi00579a030)
Interactions between the quaternary structure of the globin and the spin state of the heme in ferric mixed spin derivatives of hemoglobin.
Biochemistry
(2002)
17
3640
(doi: 10.1021/bi00610a034)
Mechanism of aminoacylation of transfer RNA. A pre-steady-state analysis of the reaction pathway catalyzed by the methionyl-tRNA synthetase of Bacillus stearothermophilus
Biochemistry
(2002)
17
5591
(doi: 10.1021/bi00619a002)
Ligand binding stoichiometries, subunit structure, and slow transitions in aminoacyl-tRNA synthetases.
Biochemistry
(2002)
16
4005
(doi: 10.1021/bi00637a011)
Enzyme hyperspecificity. Rejection of threonine by the valyl-tRNA synthetase by misacylation and hydrolytic editing
Biochemistry
(2002)
15
3342
(doi: 10.1021/bi00660a026)
Effects of engineering complementary charged residues into the hydrophobic subunit interface of tyrosyl-tRNA synthetase
Biochemistry
(2002)
26
4131
(doi: 10.1021/bi00387a058)
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)
