Proteins are dynamic molecules, relying on conformational changes to carry out function. Measurement of these conformational changes can provide insight into how function is achieved. For proteins in the solid state, this can be done by measuring the decrease in the strength of anisotropic interactions due to motion-induced fluctuations. The measurement of one-bond heteronuclear dipole-dipole coupling at magic-angle-spinning (MAS) frequencies >60 kHz is ideal for this purpose. However,...
[NMR paper] A unified heteronuclear decoupling picture in solid-state NMR under low radio-frequency amplitude and fast magic-angle-spinning frequency regime.
A unified heteronuclear decoupling picture in solid-state NMR under low radio-frequency amplitude and fast magic-angle-spinning frequency regime.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/https:--publishing.aip.org-sites-default-files-aippub-NLM-scitationblue.jpg Related Articles A unified heteronuclear decoupling picture in solid-state NMR under low radio-frequency amplitude and fast magic-angle-spinning frequency regime.
J Chem Phys. 2019 Apr 14;150(14):144201
Authors: Sharma K, Equbal A, Nielsen NC, Madhu PK
...
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04-15-2019 07:29 PM
[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] 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
Magic Angle Spinning NMR of Proteins: High-Frequency Dynamic Nuclear Polarization and H Detection
From The DNP-NMR Blog:
Magic Angle Spinning NMR of Proteins: High-Frequency Dynamic Nuclear Polarization and H Detection
Su, Y., L. Andreas, and R.G. Griffin, Magic Angle Spinning NMR of Proteins: High-Frequency Dynamic Nuclear Polarization and H Detection. Annu Rev Biochem, 2015.
http://www.ncbi.nlm.nih.gov/pubmed/25839340
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04-17-2015 08:49 PM
[NMR paper] Magic Angle Spinning NMR of Proteins: High-Frequency Dynamic Nuclear Polarization and (1)H Detection.
Magic Angle Spinning NMR of Proteins: High-Frequency Dynamic Nuclear Polarization and (1)H Detection.
Magic Angle Spinning NMR of Proteins: High-Frequency Dynamic Nuclear Polarization and (1)H Detection.
Annu Rev Biochem. 2015 Mar 30;
Authors: Su Y, Andreas L, Griffin RG
Abstract
Magic angle spinning (MAS) NMR studies of amyloid and membrane proteins and large macromolecular complexes are an important new approach to structural biology. However, the applicability of these experiments, which are based on (13)C- and...
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04-04-2015 05:31 PM
[NMR paper] Recent advances in magic angle spinning solid state NMR of membrane proteins.
Recent advances in magic angle spinning solid state NMR of membrane proteins.
Recent advances in magic angle spinning solid state NMR of membrane proteins.
Prog Nucl Magn Reson Spectrosc. 2014 Oct;82C:1-26
Authors: Wang S, Ladizhansky V
Abstract
Membrane proteins mediate many critical functions in cells. Determining their three-dimensional structures in the native lipid environment has been one of the main objectives in structural biology. There are two major NMR methodologies that allow this objective to be accomplished....
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12-03-2014 04:05 PM
[NMR paper] Solid-state NMR Spectra of lipid-anchored Proteins under Magic Angle Spinning.
Solid-state NMR Spectra of lipid-anchored Proteins under Magic Angle Spinning.
Related Articles Solid-state NMR Spectra of lipid-anchored Proteins under Magic Angle Spinning.
J Phys Chem B. 2014 Feb 11;
Authors: Nomura K, Harada E, Sugase K, Shimamoto K
Abstract
Solid-state NMR is a promising tool for elucidating membrane-related biological phenomena. We achieved the measurement of high-resolution solid-state NMR spectra for a lipid-anchored protein embedded in lipid bilayers under magic angle spinning (MAS). To date, solid-state NMR...