2005
DOI: 10.1007/s10858-005-1202-9
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NMR Assignment of Protein Rv1980c from Mycobacterium Tuberculosis

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Cited by 3 publications
(2 citation statements)
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“…Details of NMR data collection and protein backbone and side-chain resonance assignments have been reported separately. 7 Comparison of the averaged Rv1980c structure with structures found in the Protein Data Bank (PDB) using DALI 8 revealed no statistically significant similarities, and this suggests that Rv1980c defines a novel protein fold. Analysis of the ensemble of Rv1980c solution structures shown in Figure 1(b) suggests a pseudo-two-domain architecture, where the N-terminal region accounts for roughly two-thirds of the secondary structure elements in the protein.…”
Section: Rv1980c Adopts a Novel Fold Containing A β-Grasp Motifmentioning
confidence: 96%
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“…Details of NMR data collection and protein backbone and side-chain resonance assignments have been reported separately. 7 Comparison of the averaged Rv1980c structure with structures found in the Protein Data Bank (PDB) using DALI 8 revealed no statistically significant similarities, and this suggests that Rv1980c defines a novel protein fold. Analysis of the ensemble of Rv1980c solution structures shown in Figure 1(b) suggests a pseudo-two-domain architecture, where the N-terminal region accounts for roughly two-thirds of the secondary structure elements in the protein.…”
Section: Rv1980c Adopts a Novel Fold Containing A β-Grasp Motifmentioning
confidence: 96%
“…Protein expression and purification was carried out according to the previously published methods. 7,17 All NMR data were recorded on a 14.1 T Varian Inova Spectrometer (600 MHz 1 H) equipped with a triple-resonance cryogenically cooled probe. NOE restraints were generated from inter-proton distances derived from two 13 C-edited NOESY spectra (carrier set on either the aliphatic or aromatic region) and an 15 N-edited NOESY spectrum.…”
Section: Identification Of a Putative Protein-protein Interaction Surmentioning
confidence: 99%