[NMR paper] A suite of pulse sequences based on multiple sequential acquisitions at one and two radiofrequency channels for solid-state magic-angle spinning NMR studies of proteins.
A suite of pulse sequences based on multiple sequential acquisitions at one and two radiofrequency channels for solid-state magic-angle spinning NMR studies of proteins.
A suite of pulse sequences based on multiple sequential acquisitions at one and two radiofrequency channels for solid-state magic-angle spinning NMR studies of proteins.
J Biomol NMR. 2016 Jun 30;
Authors: Sharma K, Madhu PK, Mote KR
Abstract
One of the fundamental challenges in the application of solid-state NMR is its limited sensitivity, yet a majority of experiments do not make efficient use of the limited polarization available. The loss in polarization in a single acquisition experiment is mandated by the need to select out a single coherence pathway. In contrast, sequential acquisition strategies can encode more than one pathway in the same experiment or recover unused polarization to supplement a standard experiment. In this article, we present pulse sequences that implement sequential acquisition strategies on one and two radiofrequency channels with a combination of proton and carbon detection to record multiple experiments under magic-angle spinning. We show that complementary 2D experiments such as [Formula: see text] and [Formula: see text] or DARR and [Formula: see text], and 3D experiments such as [Formula: see text] and [Formula: see text], or [Formula: see text] and [Formula: see text]* can be combined in a single experiment to ensure time savings of at least 40*%. These experiments can be done under fast or slow-moderate magic-angle spinning frequencies aided by windowed [Formula: see text] acquisition and homonulcear decoupling. The pulse sequence suite is further expanded by including pathways that allow the recovery of residual polarization, the so-called 'afterglow' pathways, to encode a number of pulse sequences to aid in assignments and chemical-shift mapping.
PMID: 27364976 [PubMed - as supplied by publisher]
A suite of pulse sequences based on multiple sequential acquisitions at one and two radiofrequency channels for solid-state magic-angle spinning NMR studies of proteins
A suite of pulse sequences based on multiple sequential acquisitions at one and two radiofrequency channels for solid-state magic-angle spinning NMR studies of proteins
Abstract
One of the fundamental challenges in the application of solid-state NMR is its limited sensitivity, yet a majority of experiments do not make efficient use of the limited polarization available. The loss in polarization in a single acquisition experiment is mandated by the need to select out a single coherence pathway. In contrast, sequential acquisition strategies can encode...
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07-01-2016 03:06 AM
[NMR paper] Spectral editing at ultra-fast magic-angle-spinning in solid-state NMR: facilitating protein sequential signal assignment by HIGHLIGHT approach.
Spectral editing at ultra-fast magic-angle-spinning in solid-state NMR: facilitating protein sequential signal assignment by HIGHLIGHT approach.
Related Articles Spectral editing at ultra-fast magic-angle-spinning in solid-state NMR: facilitating protein sequential signal assignment by HIGHLIGHT approach.
J Biomol NMR. 2016 Jan 19;
Authors: Wang S, Matsuda I, Long F, Ishii Y
Abstract
This study demonstrates a novel spectral editing technique for protein solid-state NMR (SSNMR) to simplify the spectrum drastically and to reduce...
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01-20-2016 11:54 PM
Spectral editing at ultra-fast magic-angle-spinning in solid-state NMR: facilitating protein sequential signal assignment by HIGHLIGHT approach
Spectral editing at ultra-fast magic-angle-spinning in solid-state NMR: facilitating protein sequential signal assignment by HIGHLIGHT approach
Abstract
This study demonstrates a novel spectral editing technique for protein solid-state NMR (SSNMR) to simplify the spectrum drastically and to reduce the ambiguity for protein main-chain signal assignments in fast magic-angle-spinning (MAS) conditions at a wide frequency range of 40â??80Â*kHz. The approach termed HIGHLIGHT (Wang et al., in Chem Comm 51:15055â??15058, 2015) combines the reverse 13C,...
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01-19-2016 07:37 PM
[NMR paper] Magic-Angle-Spinning Solid-State NMR of Membrane Proteins.
Magic-Angle-Spinning Solid-State NMR of Membrane Proteins.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Magic-Angle-Spinning Solid-State NMR of Membrane Proteins.
Methods Enzymol. 2015;557:307-328
Authors: Baker LA, Folkers GE, Sinnige T, Houben K, Kaplan M, van der Cruijsen EA, Baldus M
Abstract
Solid-state NMR spectroscopy (ssNMR) provides increasing possibilities to examine membrane proteins in different molecular settings, ranging...
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05-08-2015 09:18 PM
[NMR paper] Multiple acquisition of magic angle spinning solid-state NMR experiments using one receiver: Application to microcrystalline and membrane protein preparations.
Multiple acquisition of magic angle spinning solid-state NMR experiments using one receiver: Application to microcrystalline and membrane protein preparations.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Multiple acquisition of magic angle spinning solid-state NMR experiments using one receiver: Application to microcrystalline and membrane protein preparations.
J Magn Reson. 2015 Apr;253:143-53
Authors: Gopinath T, Veglia G
Abstract
Solid-state NMR...
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03-24-2015 09:58 PM
Multiple acquisition of magic angle spinning solid-state NMR experiments using one receiver: Application to microcrystalline and membrane protein preparations
Multiple acquisition of magic angle spinning solid-state NMR experiments using one receiver: Application to microcrystalline and membrane protein preparations
Publication date: April 2015
Source:Journal of Magnetic Resonance, Volume 253</br>
Author(s): T. Gopinath , Gianluigi Veglia</br>
Solid-state NMR spectroscopy of proteins is a notoriously low-throughput technique. Relatively low-sensitivity and poor resolution of protein samples require long acquisition times for multidimensional NMR experiments. To speed up data acquisition, we developed a family of...
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03-20-2015 01:48 AM
[NMR paper] Multiple acquisition/multiple observation separated local field/chemical shift correlation solid-state magic angle spinning NMR spectroscopy.
Multiple acquisition/multiple observation separated local field/chemical shift correlation solid-state magic angle spinning NMR spectroscopy.
Multiple acquisition/multiple observation separated local field/chemical shift correlation solid-state magic angle spinning NMR spectroscopy.
J Magn Reson. 2014 Jun 28;245C:98-104
Authors: Das BB, Opella SJ
Abstract
Multiple acquisition spectroscopy (MACSY) experiments that enable multiple free induction decays to be recorded during individual experiments are demonstrated. In...
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07-16-2014 10:46 AM
[NMR paper] Orphan spin operators enable the acquisition of multiple 2D and 3D magic angle spinning solid-state NMR spectra.
Orphan spin operators enable the acquisition of multiple 2D and 3D magic angle spinning solid-state NMR spectra.
Related Articles Orphan spin operators enable the acquisition of multiple 2D and 3D magic angle spinning solid-state NMR spectra.
J Chem Phys. 2013 May 14;138(18):184201
Authors: Gopinath T, Veglia G
Abstract
We propose a general method that enables the acquisition of multiple 2D and 3D solid-state NMR spectra for U-(13)C, (15)N-labeled proteins. This method, called MEIOSIS (Multiple ExperIments via Orphan SpIn operatorS), makes...
A suite of pulse sequences based on multiple sequential acquisitions at one and two radiofrequency channels for solid-state magic-angle spinning NMR studies of proteins.
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