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13Cβ and NH assignments are reported for a 64 kDa complex consisting of perdeuterated (>90%) trp repressor, unlabeled operator DNA and tryptophan. of special interest
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Solution structure of the 30 kDa N-terminal domain of enzyme I of the Escherichia coli phosphoenolpyruvate: Sugar phosphotransferase system by multi-dimensional NMR
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13C-labeled samples. This is one of the largest structures solved to date using NMR methods. of special interest
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13C-labeled samples. This is one of the largest structures solved to date using NMR methods. of special interest.
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15N-labeled protein: Potential in structure determination of large proteins by NMR
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1H-labeled isoleucine, leucine and valine are incorporated into an otherwise highly deuterated protein to increase the number of NOE restraints available for structure calculations. of special interest.
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An approach to global fold determination using limited NMR data from larger proteins selectively protonated at specific residues
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Smith BO, Ito Y, Raine A, Teichmann S, Ben-Tovim L, Nietlispach D, Broadhurst RW, Terada T, Kelly M, Oschkinat K, et al. An approach to global fold determination using limited NMR data from larger proteins selectively protonated at specific residues. J Biomol NMR. 8:1996;360-368 A similar approach to that described in [36]. In addition, protonated aromatic residues are incorporated by adding these amino acids to the growth medium. Significant improvements in structures are obtained from the set of experimental NOE restraints generated from molecules labeled in this manner relative to structure obtained from NH-NH restraints only. of special interest.
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Highly deuterated proteins with protonation of the methyl groups of alanine, valine, leucine and isoleucine (γ2) can be produced by overexpression using protonated pyruvate as the sole carbon source. of special interest
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1H-δ1 methyl) isoleucine into proteins for multidimensional NMR studies
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+ binding site on the MurB enzyme by NMR
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A simple strategy for mapping the residues involved in substrate binding is presented based on changes observed in HNCO spectra in response to binding. The method does not require the chemical shifts of the protein - ligand complex to be assigned. of outstanding interest
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+ binding site on the MurB enzyme by NMR. Nat Struct Biol. 3:1996;995-997 A simple strategy for mapping the residues involved in substrate binding is presented based on changes observed in HNCO spectra in response to binding. The method does not require the chemical shifts of the protein - ligand complex to be assigned. of outstanding interest.
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Solution structure of an rRNA methyltransferase (ErmAm) that confers MLS antibiotic resistance
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Structure and ligand recognition of the phosphotyrosine binding domain of Shc
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1H dipolar splittings in proteins. On the basis of the measured splittings in ubiquitin, the principal components of the susceptibility tensor are obtained and found to be in reasonably good agreement with calculated values that include contributions only from aromatic groups and backbone peptide bonds. of special interest
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1H dipolar splittings in proteins. On the basis of the measured splittings in ubiquitin, the principal components of the susceptibility tensor are obtained and found to be in reasonably good agreement with calculated values that include contributions only from aromatic groups and backbone peptide bonds. of special interest.
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0030940339
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NMR evidence for slow collective motions in cyanometmyoglobin
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1H dipolar splittings in cyanometmyoglobin are interpreted in terms of a model in which the protein undergoes large amplitude motions from the average structure. of outstanding interest
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1H dipolar splittings in cyanometmyoglobin are interpreted in terms of a model in which the protein undergoes large amplitude motions from the average structure. of outstanding interest.
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15N-labeled proteins based on quantitative-J spectroscopy. of special interest
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15N-labeled proteins based on quantitative-J spectroscopy. of special interest.
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0030612335
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13C couplings in the structure determination of magnetically oriented macromolecules in solution
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Residual dipolar splittings are used as structural restraints in the refinement of the solution structure of a complex of the DNA-binding domain of GATA-1 and a 16mer DNA. of outstanding interest
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13C couplings in the structure determination of magnetically oriented macromolecules in solution. Nat Struct Biol. 1997; Residual dipolar splittings are used as structural restraints in the refinement of the solution structure of a complex of the DNA-binding domain of GATA-1 and a 16mer DNA. of outstanding interest.
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Defining long range order in NMR structure determination by diffusion induced relaxation anisotropy
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15N-NH bond vectors relative to the axially symmetric diffusion tensor of the molecule. This method provides a valuable source of long-range order. of outstanding interest
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15N-NH bond vectors relative to the axially symmetric diffusion tensor of the molecule. This method provides a valuable source of long-range order. of outstanding interest.
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Direct measurement of angles between bond vectors in high resolution NMR
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1Hα dipolar fields. of special interest
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1Hα dipolar fields. of special interest.
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