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Citation: Q. Zhang et al., Structural characterization of the complex of the Rev response element RNAwith a selected peptide, CHEM BIOL, 8(5), 2001, pp. 511-520
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Citation: Jw. Cave et al., Solution nuclear magnetic resonance structure of a protein disulfide oxidoreductase from Methanococcus jannaschii, PROTEIN SCI, 10(2), 2001, pp. 384-396
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Citation: M. Bastos et al., Thermodynamics of the helix-coil transition: Binding of S15 and a hybrid sequence, disulfide stabilized peptide to the S-protein, PROTEINS, 42(4), 2001, pp. 523-530
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Citation: Ca. Hawkins et al., Structural analysis of the binding modes of minor groove ligands comprisedof disubstituted benzenes, NUCL ACID R, 29(4), 2001, pp. 936-942
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Citation: Dd. Laws et al., Solid-state NMR studies of the secondary structure of a mutant prion protein fragment of 55 residues that induces neurodegeneration, P NAS US, 98(20), 2001, pp. 11686-11690
Citation: P. Rai et al., Localization of Fe2+ at an RTGR sequence within a DNA duplex explains preferential cleavage by Fe2+ and H2O2, J MOL BIOL, 312(5), 2001, pp. 1089-1101
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Citation: Sy. Lee et al., Crystal structure of activated CheY - Comparison with other activated receiver domains, J BIOL CHEM, 276(19), 2001, pp. 16425-16431
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Citation: Rh. Havlin et al., An experimental and theoretical investigation of the chemical shielding tensors of C-13(alpha) of alanine, valine, and leucine residues in solid peptides and in proteins in solution, J AM CHEM S, 123(42), 2001, pp. 10362-10369
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Citation: Sm. Rubin et al., Detection of a conformational change in maltose binding protein by Xe-129 NMR spectroscopy, J AM CHEM S, 123(35), 2001, pp. 8616-8617
Citation: Jw. Cave et al., Backbone dynamics of sequence specific recognition and binding by the yeast Pho4 bHLH domain probed by NMR, PROTEIN SCI, 9(12), 2000, pp. 2354-2365
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Citation: Sm. Rubin et al., Evidence of nonspecific surface interactions between laser-polarized xenonand myoglobin in solution, P NAS US, 97(17), 2000, pp. 9472-9475
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Citation: K. Liu et al., Deuterium-proton exchange on the native wild-type transthyretin tetramer identifies the stable core of the individual subunits and indicates mobilityat the subunit interface, J MOL BIOL, 303(4), 2000, pp. 555-565
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Citation: Sa. Robertson et al., Structure determination and binding kinetics of a DNA aptamer - Argininamide complex, BIOCHEM, 39(5), 2000, pp. 946-954
Citation: Rj. Read et De. Wemmer, Biophysical methods - Bigger, better, faster and automatically too? Editorial overview, CURR OP STR, 9(5), 1999, pp. 591-593