Band-selective universal 90° and 180° rotation pulses covering the aliphatic carbon chemical shift range for triple resonance experiments on 1.2Â*GHz spectrometers
Band-selective universal 90° and 180° rotation pulses covering the aliphatic carbon chemical shift range for triple resonance experiments on 1.2Â*GHz spectrometers
Biomolecular NMR spectroscopy requires large magnetic field strengths for high spectral resolution. Todayâ??s highest fields comprise proton Larmor frequencies of 1.2Â*GHz and even larger field strengths are to be expected in the future. In protein triple resonance experiments, various carbon bandwidths need to be excited by selective pulses including the large aliphatic chemical shift range. When the spectrometer field strength is increased, the length of these pulses has to be decreased by the same factor, resulting in higher rf-amplitudes being necessary in order to cover the required frequency region. Currently available band-selective pulses like Q3/Q5 excite a narrow bandwidth compared to the necessary rf-amplitude. Because the maximum rf-power allowed in probeheads is limited, none of the selective universal rotation pulses reported so far is able to cover the full \(^{13}\) C aliphatic region on 1.2Â*GHz spectrometers. In this work, we present band-selective 90° and 180° universal rotation pulses (SURBOP90 and SURBOP180) that have a higher ratio of selective bandwidth to maximum rf-amplitude than standard pulses. Simulations show that these pulses perform better than standard pulses, e. g. Q3/Q5, especially when rf-inhomogeneity is taken into account. The theoretical and experimental performance is demonstrated in offset profiles and by implementing the SURBOP pulses in an HNCACB experiment at 1.2Â*GHz.
[NMR paper] Bidirectional band-selective magnetization transfer along the protein backbone doubles the information content of solid-state NMR correlation experiments.
Bidirectional band-selective magnetization transfer along the protein backbone doubles the information content of solid-state NMR correlation experiments.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles Bidirectional band-selective magnetization transfer along the protein backbone doubles the information content of solid-state NMR correlation experiments.
J Biomol NMR. 2017 Nov 08;:
Authors: Jolly MM, Jarvis JA, Carravetta M, Levitt MH, Williamson...
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11-10-2017 01:30 AM
Bidirectional band-selective magnetization transfer along the protein backbone doubles the information content of solid-state NMR correlation experiments
Bidirectional band-selective magnetization transfer along the protein backbone doubles the information content of solid-state NMR correlation experiments
Abstract
Resonance assignment is the first stage towards solving the structure of a protein. This is normally achieved by the employment of separate inter and intra residue experiments. By utilising the mixed rotation and rotary recoupling (MIRROR) condition it is possible to double the information content through the efficient bidirectional transfer of magnetization from the CO to its adjacent Cα...
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11-09-2017 08:55 AM
[NMR paper] Band-selective heteronuclear dipolar recoupling with dual back-to-back pulses in rotating solids
Band-selective heteronuclear dipolar recoupling with dual back-to-back pulses in rotating solids
Publication date: Available online 6 September 2016
Source:Journal of Magnetic Resonance</br>
Author(s): Zhengfeng Zhang, Yanke Chen, Jun Yang</br>
We propose a robust band-selective heteronuclear 15N-13C recoupling method using dual back-to-back (BABA) pulses (DBP). It contains four 90° pulses in each rotor period and corresponding phase cycling on each channel (13C and 15N). DBP aims at rapid band-selective heteronuclear magnetization transfer between 15N and...
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09-22-2016 06:26 AM
[NMR paper] Measuring translational diffusion coefficients of peptides and proteins by PFG-NMR using band-selective RF pulses.
Measuring translational diffusion coefficients of peptides and proteins by PFG-NMR using band-selective RF pulses.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles Measuring translational diffusion coefficients of peptides and proteins by PFG-NMR using band-selective RF pulses.
Eur Biophys J. 2014 May 14;
Authors: Yao S, Weber DK, Separovic F, Keizer DW
Abstract
Molecular translational self-diffusion, a measure of diffusive...
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05-16-2014 08:06 PM
[NMR paper] EZ-ASSIGN, a program for exhaustive NMR chemical shift assignments of large proteins from complete or incomplete triple-resonance data.
EZ-ASSIGN, a program for exhaustive NMR chemical shift assignments of large proteins from complete or incomplete triple-resonance data.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles EZ-ASSIGN, a program for exhaustive NMR chemical shift assignments of large proteins from complete or incomplete triple-resonance data.
J Biomol NMR. 2013 Sep 11;
Authors: Zuiderweg ER, Bagai I, Rossi P, Bertelsen EB
Abstract
For several of the proteins...
[Question from NMRWiki Q&A forum] Chemical shift evolution compensation for delays flanked by hard or soft pulses
Chemical shift evolution compensation for delays flanked by hard or soft pulses
Hello all,In a typical 2D experiment, the delay "d0" (t1 increment delay in Bruker) is compensated for the chemical shift evolution that would happen during the rf pulse (hard/soft) that are applied flanking (before and after) the "d0" delay.
I could also find similar such compensations for shaped pulses before a delay in the pulse programs. These compensation factors varies for different types of pulses, e.g. 2/pi for 90 hard pulse , 0.52 for pc490120. Can someone guide me how these compensation factors...
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08-02-2012 10:48 PM
4D Non-uniformly sampled HCBCACON and 1J(NCα)-selective HCBCANCO experiments for the sequential assignment and chemical shift analysis of intrinsically disordered proteins
4D Non-uniformly sampled HCBCACON and 1J(NCα)-selective HCBCANCO experiments for the sequential assignment and chemical shift analysis of intrinsically disordered proteins
Abstract A pair of 4D NMR experiments for the backbone assignment of disordered proteins is presented. The experiments exploit 13C direct detection and non-uniform sampling of the indirectly detected dimensions, and provide correlations of the aliphatic proton (Hα, and Hβ) and carbon (Cα, Cβ) resonance frequencies to the protein backbone. Thus, all the chemical shifts regularly used to map the transient...