Hybridization of TEDOR and NCX MAS solid-state NMR experiments for simultaneous acquisition of heteronuclear correlation spectra and distance measurements
Hybridization of TEDOR and NCX MAS solid-state NMR experiments for simultaneous acquisition of heteronuclear correlation spectra and distance measurements
Magic angle spinning (MAS) solid-state NMR (ssNMR) spectroscopy is a major technique for the characterization of the structural dynamics of biopolymers at atomic resolution. However, the intrinsic low sensitivity of this technique poses significant limitations to its routine application in structural biology. Here we achieve substantial savings in experimental time using a new subclass of Polarization Optimized Experiments (POEs) that concatenate TEDOR and SPECIFIC-CP transfers into a single pulse sequence. Specifically, we designed new 2D and 3D experiments (2D TEDOR-NCX, 3D TEDOR-NCOCX, and 3D TEDOR-NCACX) to obtain distance measurements and heteronuclear chemical shift correlations for resonance assignments using only one experiment. We successfully tested these experiments on N-Acetyl-Val-Leu dipeptide, microcrystalline U-13C,15N ubiquitin, and single- and multi-span membrane proteins reconstituted in lipid membranes. These pulse sequences can be implemented on any ssNMR spectrometer equipped with standard solid-state hardware using only one receiver. Since these new POEs speed up data acquisition considerably, we anticipate their broad application to fibrillar, microcrystalline, and membrane-bound proteins.
[NMR paper] A robust heteronuclear dipolar recoupling method comparable to TEDOR for proteins in magic-angle spinning solid-state NMR.
A robust heteronuclear dipolar recoupling method comparable to TEDOR for proteins in magic-angle spinning solid-state NMR.
A robust heteronuclear dipolar recoupling method comparable to TEDOR for proteins in magic-angle spinning solid-state NMR.
J Magn Reson. 2017 Oct 31;285:79-85
Authors: Zhang Z, Li J, Chen Y, Xie H, Yang J
Abstract
In this letter, we propose a robust heteronuclear dipolar recoupling method for proteins in magic-angle spinning (MAS) solid-state NMR. This method is as simple, robust and efficient as the...
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11-12-2017 09:08 AM
A robust heteronuclear dipolar recoupling method comparable to TEDOR for proteins in magic-angle spinning solid-state NMR
A robust heteronuclear dipolar recoupling method comparable to TEDOR for proteins in magic-angle spinning solid-state NMR
Publication date: Available online 31 October 2017
Source:Journal of Magnetic Resonance</br>
Author(s): Zhengfeng Zhang, Jianping Li, Yanke Chen, Huayong Xie, Jun Yang</br>
In this letter, we propose a robust heteronuclear dipolar recoupling method for proteins in magic-angle spinning (MAS) solid-state NMR. This method is as simple, robust and efficient as the well-known TEDOR in the aspect of magnetization transfer between 15N and 13C....
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11-01-2017 05:51 AM
[NMR paper] Simultaneous acquisition of 2D and 3D solid-state NMR experiments for sequential assignment of oriented membrane protein samples.
Simultaneous acquisition of 2D and 3D solid-state NMR experiments for sequential assignment of oriented membrane protein samples.
Related Articles Simultaneous acquisition of 2D and 3D solid-state NMR experiments for sequential assignment of oriented membrane protein samples.
J Biomol NMR. 2015 Mar 7;
Authors: Gopinath T, Mote KR, Veglia G
Abstract
We present a new method called DAISY (Dual Acquisition orIented ssNMR spectroScopY) for the simultaneous acquisition of 2D and 3D oriented solid-state NMR experiments for membrane...
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03-10-2015 07:22 PM
Simultaneous acquisition of 2D and 3D solid-state NMR experiments for sequential assignment of oriented membrane protein samples
Simultaneous acquisition of 2D and 3D solid-state NMR experiments for sequential assignment of oriented membrane protein samples
Abstract
We present a new method called DAISY (Dual Acquisition orIented ssNMR spectroScopY) for the simultaneous acquisition of 2D and 3D oriented solid-state NMR experiments for membrane proteins reconstituted in mechanically or magnetically aligned lipid bilayers. DAISY utilizes dual acquisition of sine and cosine dipolar or chemical shift coherences and long living 15N longitudinal polarization to obtain two...
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03-08-2015 01:07 AM
3D DUMAS: Simultaneous acquisition of three-dimensional magic angle spinning solid-state NMR experiments of proteins
3D DUMAS: Simultaneous acquisition of three-dimensional magic angle spinning solid-state NMR experiments of proteins
July 2012
Publication year: 2012
Source:Journal of Magnetic Resonance, Volume 220</br>
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Using the DUMAS (Dual acquisition Magic Angle Spinning) solid-state NMR approach, we created new pulse schemes that enable the simultaneous acquisition of three dimensional (3D) experiments on uniformly 13C, 15N labeled proteins. These new experiments exploit the simultaneous cross-polarization (SIM-CP) from 1H to 13C and 15N to acquire two 3D experiments...
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02-03-2013 10:13 AM
Solid state NMR of proteins at high MAS frequencies: symmetry-based mixing and simultaneous acquisition of chemical shift correlation spectra
Solid state NMR of proteins at high MAS frequencies: symmetry-based mixing and simultaneous acquisition of chemical shift correlation spectra
Abstract We have carried out chemical shift correlation experiments with symmetry-based mixing sequences at high MAS frequencies and examined different strategies to simultaneously acquire 3D correlation spectra that are commonly required in the structural studies of proteins. The potential of numerically optimised symmetry-based mixing sequences and the simultaneous recording of chemical shift correlation spectra such as: 3D NCAC and 3D NHH...
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11-29-2012 03:14 AM
3D DUMAS: Simultaneous Acquisition of Three-Dimensional Magic Angle Spinning Solid-State NMR Experiments of Proteins
3D DUMAS: Simultaneous Acquisition of Three-Dimensional Magic Angle Spinning Solid-State NMR Experiments of Proteins
Publication year: 2012
Source:Journal of Magnetic Resonance</br>
T. Gopinath, Gianluigi Veglia</br>
Using the DUMAS (Dual acquisition Magic Angle Spinning) solid-state NMR approach, we created new pulse schemes that enable the simultaneous acquisition of three dimensional (3D) experiments on uniformly 13C, 15N labeled proteins. These new experiments exploit the simultaneous cross-polarization (SIM-CP) from 1H to 13C and 15N to acquire two 3D experiments...
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04-26-2012 08:10 PM
Four-dimensional heteronuclear correlation experiments for chemical shift assignment of solid proteins
Four-dimensional heteronuclear correlation experiments for chemical shift assignment of solid proteins
W. Trent Franks, Kathryn D. Kloepper, Benjamin J. Wylie and Chad M. Rienstra
Journal of Biomolecular NMR; 2007; 39(2); pp 107 - 131
Abstract:
Chemical shift assignment is the first step in all established protocols for structure determination of uniformly labeled proteins by NMR. The explosive growth in recent years of magic-angle spinning (MAS) solid-state NMR (SSNMR) applications is largely attributable to improved methods for backbone and side-chain chemical shift correlation...