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- Currently displaying 20741 - 20760 of 27924 publications
Ligand binding stoichiometries, subunit structure, and slow transitions in aminoacyl-tRNA synthetases.
– Biochemistry
(2002)
16,
4005
(doi: 10.1021/bi00637a011)
Subunit interactions in the methionyl-tRNA synthetase of Bacillus stearothermophilus.
– Biochemistry
(2002)
15,
243
(doi: 10.1021/bi00647a001)
SOLID-STATE NMR-STUDIES OF THE ALUMINOPHOSPHATE MOLECULAR-SIEVE ALPO4-18
– Journal of Physical Chemistry
(2002)
97,
10385
(doi: 10.1021/j100142a020)
Synthesis and reducibility of homo-2-methoxyazocines and their benzo-fused derivatives. An examination of heteroatomic influences on the possible generation of 9C-10.pi. homoaromatic dianions
– The Journal of Organic Chemistry
(2002)
43,
4712
(doi: 10.1021/jo00419a007)
Editing mechanisms in aminoacylation of tRNA:ATP consumption and the binding of aminoacyl-tRNA by elongation factor Tu
– Biochemistry
(2002)
16,
4731
(doi: 10.1021/bi00640a031)
SI-29 MAGIC-ANGLE-SPINNING NMR-SPECTROSCOPY QUANTITATIVELY MONITORS THE DOUBLE-CHAIN TRIPLE-CHAIN INTERGROWTHS IN HYDROUS SILICATES
– Journal of the American Chemical Society
(2002)
113,
7100
(doi: 10.1021/ja00019a002)
Mechanism of aminoacylation of tRNA. Proof of the aminoacyl adenylate pathway for the isoleucyl- and tyrosyl-tRNA synthetases from Escherichia coli K12
– Biochemistry
(2002)
15,
818
(doi: 10.1021/bi00649a014)
A model for strongly hindered molecular reorientation in liquids
– Journal of Physical Chemistry
(2002)
88,
6514
(doi: 10.1021/j150670a013)
X-ray diffraction and 13C solid-state NMR studies of the solvate of tetra(C-undecyl)calix[4]resorcinarene with dimethylacetamideElectronic supplementary information (ESI) available: Positional parameters, bond lengths and angles, and atomic displacement parameters of CAV11/DMA, and crystallographic data in .cif format (CCDC reference number 170110). See http://www.rsc.org/suppdata/cp/b1/b107416b/
– Physical Chemistry Chemical Physics
(2002)
4,
2387
(doi: 10.1039/b107416b)
Hydrogen bonding and the structure of substituted quinoxalines: solid-state NMR and single-crystal x-ray diffraction studies
– Journal of Physical Chemistry
(2002)
97,
1862
(doi: 10.1021/j100111a024)
Tetracyanoethylene Addition to Iron Tricarbonyl Complexes of Substituted Cyclooctatetraenes. Regioselectivity Considerations during Formation of the 2,3,4,10-Tetrahapto Adducts
– Journal of the American Chemical Society
(2002)
97,
4658
(doi: 10.1021/ja00849a031)
Simulation of water around a model protein helix. 1. Two-dimensional projections of solvent structure
– Journal of Physical Chemistry
(2002)
97,
2982
(doi: 10.1021/j100114a026)
Structural studies on peptides corresponding to mutants of the major alpha-helix of barnase.
– Biochemistry
(2002)
33,
10013
(doi: 10.1021/bi00199a027)
H-1 MAGIC-ANGLE-SPINNING NMR-STUDIES OF THE ADSORPTION OF ALCOHOLS ON MOLECULAR-SIEVE CATALYSTS
– The Journal of Physical Chemistry
(2002)
95,
235
(doi: 10.1021/j100154a046)
Ligand binding and enzymic catalysis coupled through subunits in tyrosyl-tRNA synthetase.
– Biochemistry
(2002)
14,
13
(doi: 10.1021/bi00672a003)
Cooperative Elements in Protein Folding Monitored by Electrospray Ionization Mass Spectrometry
– Journal of the American Chemical Society
(2002)
117,
7548
(doi: 10.1021/ja00133a030)
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)
Exploring the energy surface of protein folding by structure-reactivity relationships and engineered proteins: observation of Hammond behavior for the gross structure of the transition state and anti-Hammond behavior for structural elements for unfolding/folding of barnase.
– Biochemistry
(2002)
34,
6805
(doi: 10.1021/bi00020a027)
Free energies of hydrolysis of amides and peptides in aqueous solution at 25 degrees.
– J Am Chem Soc
(2002)
93,
3499
(doi: 10.1021/ja00743a034)
Effects of engineering complementary charged residues into the hydrophobic subunit interface of tyrosyl-tRNA synthetase. Appendix: Kinetic analysis of dimeric enzymes that reversibly dissociate into inactive subunits.
– Biochemistry
(2002)
26,
4131
(doi: 10.1021/bi00387a058)