Related Articles3D TROSY-HNCA(coded)CB and TROSY-HNCA(coded)CO experiments: triple resonance NMR experiments with two sequential connectivity pathways and high sensitivity.
J Biomol NMR. 2004 Mar;28(3):289-94
Authors: Ritter C, Lührs T, Kwiatkowski W, Riek R
The concept of chemical shift-coding monitors chemical shifts in multi-dimensional NMR experiments without additional polarization transfer elements and evolution periods. The chemical shifts are coded in the line-shape of the cross-peak through an apparent scalar coupling dependent upon the chemical shift. This concept is applied to the three-dimensional triple-resonance experiment HNCA adding the information of (13)C(beta) or (13)C' chemical shifts. On average, the proposed TROSY-HNCA(coded)CB experiment is a factor of 2 less sensitive than the HNCA experiment. However, it contains correlations via the chemical shifts of both (13)C(alpha) and (13)C(beta), and provides up to three times higher resolution along the (13)C(alpha) chemical shift axis. Thus, it dramatically reduces ambiguities in linking the spin systems of adjacent residues in the protein sequence during the sequential assignment. The TROSY-HNCA(coded)CO experiment which is conceptually similar contains correlations via the chemical shifts of (13)C(alpha) and (13)C' without major signal losses. The proposed triple resonance experiments are applied to a approximately 70% (2)H, approximately 85% (13)C,(15)N labeled protein with a molecular weight of 25 kDa.
Multiplet-filtered and gradient-selected zero-quantum TROSY experiments for 13C1H3 methyl groups in proteins
Multiplet-filtered and gradient-selected zero-quantum TROSY experiments for 13C1H3 methyl groups in proteins
Abstract Multiplet-filtered and gradient-selected heteronuclear zero-quantum coherence (gsHZQC) TROSY experiments are described for measuring 1Hâ??13C correlations for 13CH3 methyl groups in proteins. These experiments provide improved suppression of undesirable, broad outer components of the heteronuclear zero-quantum multiplet in medium-sized proteins, or in flexible sites of larger proteins, compared to previously described HZQC sequences (Tugarinov et al. in J Am Chem Soc...
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09-17-2011 10:20 AM
[NMRpipe Yahoo group] Re: phase problem with trosy-hncacb
Re: phase problem with trosy-hncacb
It is best not use automated baseline correction before at least two dimensions have been transformed. Same with LP ... also, best not to use LP until all the
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05-27-2011 10:40 AM
[NMRpipe Yahoo group] phase problem with trosy-hncacb
phase problem with trosy-hncacb
Dear All: I have this strange phase problem with trosy-hncacb collected on a bruker machine. the HC and HN projection looks good. However, Using the phase
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03-15-2011 05:56 AM
Pseudo-4D triple resonance experiments to resolve HN overlap in the backbone assignment of unfolded proteins
Pseudo-4D triple resonance experiments to resolve HN overlap in the backbone assignment of unfolded proteins
Abstract The solution NMR resonance assignment of the protein backbone is most commonly carried out using triple resonance experiments that involve 15N and 1HN resonances. The assignment becomes problematic when there is resonance overlap of 15Nâ??1HN cross peaks. For such residues, one cannot unambiguously link the â??leftâ?? side of the NH root to the â??rightâ?? side, and the residues associated with such overlapping HN resonances remain often unassigned. Here we present a...
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12-31-2010 08:38 PM
HNCA-TOCSY-CANH experiments with alternate 13C-12C labeling: a set of 3D experiment w
HNCA-TOCSY-CANH experiments with alternate 13C-12C labeling: a set of 3D experiment with unique supra-sequential information for mainchain resonance assignment
Abstract Described here is a set of three-dimensional (3D) NMR experiments that rely on CACA-TOCSY magnetization transfer via the weak
3 \textJ\textCa\textCa coupling. These pulse sequences, which resemble recently described 13C detected CACA-TOCSY (Takeuchi et al. 2010) experiments, are recorded in 1H2O, and use 1H excitation and detection. These experiments require alternate 13C-12C labeling together with perdeuteration,...
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11-27-2010 07:34 PM
[NMR paper] Assignment of amide proton signals by combined evaluation of HN, NN and HNCA MAS-NMR
Assignment of amide proton signals by combined evaluation of HN, NN and HNCA MAS-NMR correlation spectra.
Related Articles Assignment of amide proton signals by combined evaluation of HN, NN and HNCA MAS-NMR correlation spectra.
J Biomol NMR. 2003 Mar;25(3):217-23
Authors: van Rossum BJ, Castellani F, Pauli J, Rehbein K, Hollander J, de Groot HJ, Oschkinat H
In this paper, we present a strategy for the (1)H(N) resonance assignment in solid-state magic-angle spinning (MAS) NMR, using the alpha-spectrin SH3 domain as an example. A novel 3D...
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11-24-2010 09:01 PM
[NMR paper] A sequential HNCA NMR pulse sequence for protein backbone assignment.
A sequential HNCA NMR pulse sequence for protein backbone assignment.
Related Articles A sequential HNCA NMR pulse sequence for protein backbone assignment.
J Magn Reson. 2001 May;150(1):100-4
Authors: Meissner A, Sĝrensen OW
The conventional HNCA pulse sequence suffers from the ambiguity that it cannot distinguish inter- and intraresidue correlations because the one-bond and two-bond J(NC(alpha)) coupling constants are of similar magnitude. This paper presents a novel pulse sequence, sequential HNCA, that leads to a spectrum exhibiting...
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11-19-2010 08:32 PM
[NMR paper] Protein dynamics measurements by TROSY-based NMR experiments.
Protein dynamics measurements by TROSY-based NMR experiments.
Related Articles Protein dynamics measurements by TROSY-based NMR experiments.
J Magn Reson. 2000 Apr;143(2):423-6
Authors: Zhu G, Xia Y, Nicholson LK, Sze KH
The described TROSY-based experiments for investigating backbone dynamics of proteins make it possible to elucidate internal motions in large proteins via measurements of T(1), T(2), and NOE of backbone (15)N nuclei. In our proposed sequences, the INEPT sequence is eliminated and the PEP sequence is replaced by the ST2-PT...
3D TROSY-HNCA(coded)CB and TROSY-HNCA(coded)CO experiments: triple resonance NMR expe
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