scholarly article | Q13442814 |
P6179 | Dimensions Publication ID | 1008216336 |
P356 | DOI | 10.1007/S10858-008-9285-8 |
P2888 | exact match | https://scigraph.springernature.com/pub.10.1007/s10858-008-9285-8 |
P698 | PubMed publication ID | 19002386 |
P2093 | author name string | Vitali Tugarinov | |
Chenyun Guo | |||
P2860 | cites work | Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution | Q24649924 |
Crystal structure of Escherichia coli malate synthase G complexed with magnesium and glyoxylate at 2.0 A resolution: mechanistic implications | Q27621745 | ||
Rapid data collection for protein structure determination by NMR spectroscopy | Q27645025 | ||
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Simultaneous detection of amide and methyl correlations using a time shared NMR experiment: application to binding epitope mapping | Q30157885 | ||
Simultaneous acquisition of [13C,15N]- and [15N,15N]-separated 4D gradient-enhanced NOESY spectra in proteins | Q30194097 | ||
1H(C) and 1H(N) total NOE correlations in a single 3D NMR experiment. 15N and 13C time-sharing in t1 and t2 dimensions for simultaneous data acquisition. | Q30333500 | ||
A simultaneous (15)N, (1)H- and (13)C, (1)H-HSQC with sensitivity enhancement and a heteronuclear gradient echo | Q30558652 | ||
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Methyl groups as probes of structure and dynamics in NMR studies of high-molecular-weight proteins | Q36216432 | ||
A general enhancement scheme in heteronuclear multidimensional NMR employing pulsed field gradients | Q36732974 | ||
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Four-dimensional NMR spectroscopy of a 723-residue protein: chemical shift assignments and secondary structure of malate synthase g. | Q44109769 | ||
Cross-correlated relaxation enhanced 1H[bond]13C NMR spectroscopy of methyl groups in very high molecular weight proteins and protein complexes | Q44554807 | ||
An isotope labeling strategy for methyl TROSY spectroscopy | Q47228423 | ||
Time-saving methods for heteronuclear multidimensional NMR of ((13)C, (15)N) doubly labeled proteins | Q47740747 | ||
Improved 1HN-detected triple resonance TROSY-based experiments | Q47775032 | ||
An NMR experiment for simultaneous TROSY-based detection of amide and methyl groups in large proteins. | Q53534069 | ||
Determination of all nOes in 1H-13C-Me-ILV-U-2H-15N proteins with two time-shared experiments. | Q54469823 | ||
A robust and cost-effective method for the production of Val, Leu, Ile (delta 1) methyl-protonated 15N-, 13C-, 2H-labeled proteins | Q57851005 | ||
Global Folds of Highly Deuterated, Methyl-Protonated Proteins by Multidimensional NMR† | Q57851041 | ||
Selective Methyl Group Protonation of Perdeuterated Proteins | Q57851078 | ||
P433 | issue | 1 | |
P304 | page(s) | 21-30 | |
P577 | publication date | 2008-11-11 | |
P1433 | published in | Journal of Biomolecular NMR | Q3186900 |
P1476 | title | Identification of HN-methyl NOEs in large proteins using simultaneous amide-methyl TROSY-based detection | |
P478 | volume | 43 |
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Q46093940 | Methyl-detected 'out-and-back' NMR experiments for simultaneous assignments of Alabeta and Ilegamma2 methyl groups in large proteins |
Q30366295 | NMR approaches in structure-based lead discovery: recent developments and new frontiers for targeting multi-protein complexes |
Q38121298 | NMR methods for structural studies of large monomeric and multimeric proteins |
Q38188673 | Practical aspects of NMR signal assignment in larger and challenging proteins |
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Q37422910 | Time-shared HSQC-NOESY for accurate distance constraints measured at high-field in (15)N-(13)C-ILV methyl labeled proteins |
Q61949289 | Time-shared NMR experiments |
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