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Oganesyan, V.S., et al., A combined EPR and MD simulation study of a nitroxyl spin label with restricted internal mobility sensitive to protein dynamics. J. Magn. Reson., 2017. 274: p. 24-35.
EPR studies combined with fully atomistic Molecular Dynamics (MD) simulations and an MD-EPR simulation method provide evidence for intrinsic low rotameric mobility of a nitroxyl spin label, Rn, compared to the more widely employed label MTSL (R1). Both experimental and modelling results using two structurally different sites of attachment to Myoglobin show that the EPR spectra of Rn are more sensitive to the local protein environment than that of MTSL. This study reveals the potential of using the Rn spin label as a reporter of protein motions.
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Nuclear spin-lattice relaxation in nitroxide spin-label EPR
From The DNP-NMR Blog:
Nuclear spin-lattice relaxation in nitroxide spin-label EPR
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Marsh, D., Nuclear spin-lattice relaxation in nitroxide spin-label EPR. J Magn Reson, 2016. 272: p. 166-171.
https://www.ncbi.nlm.nih.gov/pubmed/27712989
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12-02-2016 07:56 PM
[NMR paper] A combined EPR and MD simulation study of a nitroxyl spin label with restricted internal mobility sensitive to protein dynamics
A combined EPR and MD simulation study of a nitroxyl spin label with restricted internal mobility sensitive to protein dynamics
Publication date: January 2017
Source:Journal of Magnetic Resonance, Volume 274</br>
Author(s): Vasily S. Oganesyan, Fatima Chami, Gaye F. White, Andrew J. Thomson</br>
EPR studies combined with fully atomistic Molecular Dynamics (MD) simulations and an MD-EPR simulation method provide evidence for intrinsic low rotameric mobility of a nitroxyl spin label, Rn, compared to the more widely employed label MTSL (R1). Both experimental...
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11-19-2016 08:35 PM
[NMR paper] Metabolic Effects of a 24-Week Energy-Restricted Intervention Combined with Low or High Dairy Intake in Overweight Women: An NMR-Based Metabolomics Investigation.
Metabolic Effects of a 24-Week Energy-Restricted Intervention Combined with Low or High Dairy Intake in Overweight Women: An NMR-Based Metabolomics Investigation.
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Nutrients. 2016;8(3)
Authors: Zheng H, Lorenzen JK, Astrup A, Larsen LH, Yde CC, Clausen MR, Bertram HC
Abstract
We investigated the effect of a 24-week energy-restricted intervention with low...
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02-27-2016 12:52 AM
Integrated analysis of the conformation of a protein-linked spin label by crystallography, EPR and NMR spectroscopy
Integrated analysis of the conformation of a protein-linked spin label by crystallography, EPR and NMR spectroscopy
Abstract Long-range structural information derived from paramagnetic relaxation enhancement observed in the presence of a paramagnetic nitroxide radical is highly useful for structural characterization of globular, modular and intrinsically disordered proteins, as well as proteinā??protein and protein-DNA complexes. Here we characterized the conformation of a spin-label attached to the homodimeric protein CylR2 using a combination of X-ray crystallography, electron...
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01-31-2011 06:03 AM
NMR Spectroscopy and Molecular Dynamics Simulation of r(CCGCUGCGG)2 Reveal a Dynamic UU Internal Loop Found in Myotonic Dystrophy Type 1
NMR Spectroscopy and Molecular Dynamics Simulation of r(CCGCUGCGG)2 Reveal a Dynamic UU Internal Loop Found in Myotonic Dystrophy Type 1
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/bi101896j/aop/images/medium/bi-2010-01896j_0004.gif
Biochemistry
DOI: 10.1021/bi101896j
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/OhiVTgV2ZTI
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01-14-2011 01:59 AM
NMR Spectroscopy and Molecular Dynamics Simulation of r(CCGCUGCGG)2 Reveal a Dynamic UU Internal Loop Found in Myotonic Dystrophy Type 1.
NMR Spectroscopy and Molecular Dynamics Simulation of r(CCGCUGCGG)2 Reveal a Dynamic UU Internal Loop Found in Myotonic Dystrophy Type 1.
NMR Spectroscopy and Molecular Dynamics Simulation of r(CCGCUGCGG)2 Reveal a Dynamic UU Internal Loop Found in Myotonic Dystrophy Type 1.
Biochemistry. 2011 Jan 4;
Authors: Parkesh R, Disney MD, Fountain M
The NMR structure of an RNA with a copy of the 5'CUG/3'GUC motif found in the triplet repeating disorder myotonic dystrophy type 1 (DM1) is disclosed. The lowest energy conformation of the UU pair is a single...
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01-06-2011 11:21 AM
[NMR paper] Side chain dynamics in unfolded protein states: an NMR based 2H spin relaxation study
Side chain dynamics in unfolded protein states: an NMR based 2H spin relaxation study of delta131delta.
Related Articles Side chain dynamics in unfolded protein states: an NMR based 2H spin relaxation study of delta131delta.
J Am Chem Soc. 2003 Feb 19;125(7):1748-58
Authors: Choy WY, Shortle D, Kay LE
NMR relaxation data on disordered proteins can provide insight into both structural and dynamic properties of these molecules. Because of chemical shift degeneracy in correlation spectra, detailed site-specific analyses of side chain dynamics...
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11-24-2010 09:01 PM
[NMR paper] Determination of local protein structure by spin label difference 2D NMR: the region
Determination of local protein structure by spin label difference 2D NMR: the region neighboring Asp61 of subunit c of the F1F0 ATP synthase.
Related Articles Determination of local protein structure by spin label difference 2D NMR: the region neighboring Asp61 of subunit c of the F1F0 ATP synthase.
Biochemistry. 1995 Feb 7;34(5):1635-45
Authors: Girvin ME, Fillingame RH
Purified subunit c from the H(+)-transporting F1F0 ATP synthase of Escherichia coli folds as an antiparallel pair of extended helices in a solution of...
A combined EPR and MD simulation study of a nitroxyl spin label with restricted internal mobility sensitive to protein dynamics
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