Identification of HN-methyl NOEs in large proteins using simultaneous amide-methyl TROSY-based detection

scientific article published on 11 November 2008

Identification of HN-methyl NOEs in large proteins using simultaneous amide-methyl TROSY-based detection is …
instance of (P31):
scholarly articleQ13442814

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P6179Dimensions Publication ID1008216336
P356DOI10.1007/S10858-008-9285-8
P2888exact matchhttps://scigraph.springernature.com/pub.10.1007/s10858-008-9285-8
P698PubMed publication ID19002386

P2093author name stringVitali Tugarinov
Chenyun Guo
P2860cites workAttenuated 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 solutionQ24649924
Crystal structure of Escherichia coli malate synthase G complexed with magnesium and glyoxylate at 2.0 A resolution: mechanistic implicationsQ27621745
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Simultaneous detection of amide and methyl correlations using a time shared NMR experiment: application to binding epitope mappingQ30157885
Simultaneous acquisition of [13C,15N]- and [15N,15N]-separated 4D gradient-enhanced NOESY spectra in proteinsQ30194097
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 echoQ30558652
Solution NMR-derived global fold of a monomeric 82-kDa enzymeQ33756699
Methyl groups as probes of structure and dynamics in NMR studies of high-molecular-weight proteinsQ36216432
A general enhancement scheme in heteronuclear multidimensional NMR employing pulsed field gradientsQ36732974
Simultaneous CT-13C and VT-15N chemical shift labelling: application to 3D NOESY-CH3NH and 3D 13C,15N HSQC-NOESY-CH3NH.Q39555754
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 complexesQ44554807
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Time-saving methods for heteronuclear multidimensional NMR of ((13)C, (15)N) doubly labeled proteinsQ47740747
Improved 1HN-detected triple resonance TROSY-based experimentsQ47775032
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 proteinsQ57851005
Global Folds of Highly Deuterated, Methyl-Protonated Proteins by Multidimensional NMR†Q57851041
Selective Methyl Group Protonation of Perdeuterated ProteinsQ57851078
P433issue1
P304page(s)21-30
P577publication date2008-11-11
P1433published inJournal of Biomolecular NMRQ3186900
P1476titleIdentification of HN-methyl NOEs in large proteins using simultaneous amide-methyl TROSY-based detection
P478volume43

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cites work (P2860)
Q43038562A 3D time-shared NOESY experiment designed to provide optimal resolution for accurate assignment of NMR distance restraints in large proteins
Q46093940Methyl-detected 'out-and-back' NMR experiments for simultaneous assignments of Alabeta and Ilegamma2 methyl groups in large proteins
Q30366295NMR approaches in structure-based lead discovery: recent developments and new frontiers for targeting multi-protein complexes
Q38121298NMR methods for structural studies of large monomeric and multimeric proteins
Q38188673Practical aspects of NMR signal assignment in larger and challenging proteins
Q84987691Simultaneous measurement of ¹H-¹⁵N and methyl ¹Hm-¹³Cm residual dipolar couplings in large proteins
Q37422910Time-shared HSQC-NOESY for accurate distance constraints measured at high-field in (15)N-(13)C-ILV methyl labeled proteins
Q61949289Time-shared NMR experiments
Q42695740Time-shared experiments for efficient assignment of triple-selectively labeled proteins

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