[NMR paper] Carbon-detected deuterium solid-state NMR rotating frame relaxation measurements for protein methyl groups under magic angle spinning
Carbon-detected deuterium solid-state NMR rotating frame relaxation measurements for protein methyl groups under magic angle spinning
Deuterium rotating frame solid-state NMR relaxation measurements (²H R(1?)) are important tools in quantitative studies of molecular dynamics. We demonstrate how ²H to ^(13)C cross-polarization (CP) approaches under 10-40 kHz magic angle spinning rates can be combined with the ²H R(1?) blocks to allow for extension of deuterium rotating frame relaxation studies to methyl groups in biomolecules. This extension permits detection on the ^(13)C nuclei and,...
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[NMR paper] Protein-Protein Interfaces Probed by Methyl-Labeling and Proton-Detected Solid-State NMR Spectroscopy.
Protein-Protein Interfaces Probed by Methyl-Labeling and Proton-Detected Solid-State NMR Spectroscopy.
Related Articles Protein-Protein Interfaces Probed by Methyl-Labeling and Proton-Detected Solid-State NMR Spectroscopy.
Chemphyschem. 2018 Jun 19;:
Authors: Zinke M, Fricke P, Lange S, Zinn-Justin S, Lange A
Abstract
Proton detection and fast magic-angle spinning have advanced biological solid-state NMR, allowing for the backbone assignment of complex protein assemblies with high sensitivity and resolution. However, so far no...
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06-20-2018 08:56 PM
[NMR paper] Proton-Detected NMR Spectroscopy of Nanodisc-Embedded Membrane Proteins: MAS Solid-State vs. Solution-State Methods.
Proton-Detected NMR Spectroscopy of Nanodisc-Embedded Membrane Proteins: MAS Solid-State vs. Solution-State Methods.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Proton-Detected NMR Spectroscopy of Nanodisc-Embedded Membrane Proteins: MAS Solid-State vs. Solution-State Methods.
J Phys Chem B. 2017 Jul 24;:
Authors: Lakomek NA, Frey L, Bibow S, Böckmann A, Riek R, Meier BH
Abstract
The structural and dynamical characterization of membrane proteins...
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07-25-2017 07:46 PM
Dynamics of Methyl Groups in Membrane Proteins Studied by Deterium Solid State NMR Relaxation
Dynamics of Methyl Groups in Membrane Proteins Studied by Deterium Solid State NMR Relaxation
Publication date: 16 February 2016
Source:Biophysical Journal, Volume 110, Issue 3, Supplement 1</br>
Author(s): Xiaolin Xu, Andrey V. Struts, Aswini Kumar Giri, Trivikram R. Molugu, Charitha Guruge, Samira Faylough, Carolina L. Nascimento, Nasri Nesnas, Victor J. Hruby, Michael F. Brown</br>
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02-17-2016 07:50 PM
[NMR paper] A straightforward method for stereospecific assignment of val and leu prochiral methyl groups by solid-state NMR: Scrambling in the [2-(13)C]Glucose labeling scheme.
A straightforward method for stereospecific assignment of val and leu prochiral methyl groups by solid-state NMR: Scrambling in the Glucose labeling scheme.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles A straightforward method for stereospecific assignment of val and leu prochiral methyl groups by solid-state NMR: Scrambling in the Glucose labeling scheme.
J Magn Reson. 2013 Jan 4;228C:45-49
Authors: Lv G, Faßhuber HK, Loquet A, Demers JP, Vijayan V, Giller K, Becker S, Lange A
...
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02-03-2013 10:19 AM
A straightforward method for stereospecific assignment of val and leu prochiral methyl groups by solid-state NMR: Scrambling in the [2-13C]Glucose labeling scheme
A straightforward method for stereospecific assignment of val and leu prochiral methyl groups by solid-state NMR: Scrambling in the Glucose labeling scheme
Available online 4 January 2013
Publication year: 2013
Source:Journal of Magnetic Resonance</br>
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The unambiguous stereospecific assignment of the prochiral methyl groups in Val and Leu plays an important role in the structural investigation of proteins by NMR. Here, we present a straightforward method for their stereospecific solid-state NMR assignment based on Glucose (Glc) as the sole carbon source during...
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01-08-2013 09:23 AM
Selective 1H-13C NMR spectroscopy of methyl groups in residually protonated samples of large proteins
Selective 1H-13C NMR spectroscopy of methyl groups in residually protonated samples of large proteins
Abstract Methyl 13CHD2 isotopomers of all methyl-containing amino-acids can be observed in residually protonated samples of large proteins obtained from -glucose/D2O-based bacterial media, with sensitivity sufficient for a number of NMR applications. Selective detection of some subsets of methyl groups (Alaβ, Thrγ2) is possible using simple â??out-and-backâ?? NMR methodology. Such selective methyl-detected â??out-and-backâ?? NMR experiments allow complete assignments of threonine γ2...
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01-09-2011 12:46 PM
High Resolution 1H Detected 1H,13C Correlation Spectra in MAS Solid-State NMR using Deuterated Proteins with Selective 1H,2H Isotopic Labeling of Methyl Groups
High Resolution <SUP>1</SUP>H Detected <SUP>1</SUP>H,<SUP>13</SUP>C Correlation Spectra in MAS Solid-State NMR using Deuterated Proteins with Selective <SUP>1</SUP>H,<SUP>2</SUP>H Isotopic Labeling of Methyl Groups
Vipin Agarwal, Anne Diehl, Nikolai Skrynnikov, and Bernd Reif
J. Am. Chem. Soc.; 2006; 128(39) pp 12620 - 12621;
Abstract:
MAS solid-state NMR experiments applied to biological solids are still hampered by low sensitivity and resolution. In this work, we employ a deuteration scheme in which individual methyl groups are selectively protonated. This labeling scheme...
Accessing Methyl Groups in Proteins via 1H-detected MAS Solid-state NMR Spectroscopy Employing Random ... - Nature.com
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