Related ArticlesMapping Membrane Protein Backbone Dynamics: A Comparison of Site-Directed Spin Labeling with NMR (15)N-Relaxation Measurements.
Biophys J. 2014 Oct 7;107(7):1697-1702
Authors: Lo RH, Kroncke BM, Solomon TL, Columbus L
Abstract
The ability to detect nanosecond backbone dynamics with site-directed spin labeling (SDSL) in soluble proteins has been well established. However, for membrane proteins, the nitroxide appears to have more interactions with the protein surface, potentially hindering the sensitivity to backbone motions. To determine whether membrane protein backbone dynamics could be mapped with SDSL, a nitroxide was introduced at 55 independent sites in a model polytopic membrane protein, TM0026. Electron paramagnetic resonance spectral parameters were compared with NMR (15)N-relaxation data. Sequential scans revealed backbone dynamics with the same trends observed for the R1 relaxation rate, suggesting that nitroxide dynamics remain coupled to the backbone on membrane proteins.
PMID: 25296323 [PubMed - as supplied by publisher]
Mapping Membrane Protein Backbone Dynamics: A Comparison of Site-Directed Spin Labeling with NMR 15N-Relaxation Measurements
Mapping Membrane Protein Backbone Dynamics: A Comparison of Site-Directed Spin Labeling with NMR 15N-Relaxation Measurements
Publication date: 7 October 2014
Source:Biophysical Journal, Volume 107, Issue 7</br>
Author(s): Ryan*H. Lo , Brett*M. Kroncke , Tsega*L. Solomon , Linda Columbus</br>
The ability to detect nanosecond backbone dynamics with site-directed spin labeling (SDSL) in soluble proteins has been well established. However, for membrane proteins, the nitroxide appears to have more interactions with the protein surface, potentially hindering the...
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[NMR paper] Mapping the UDP-N-acetylglucosamine regulatory site of human glucosamine-6P synthase by saturation-transfer difference NMR and site-directed mutagenesis.
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[NMR paper] Carbon Relaxation in (13)C(?)-H(?) and (13)C(?)-D(?) Spin Pairs as a Probe of Backbone Dynamics in Proteins.
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http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Carbon Relaxation in (13)C(?)-H(?) and (13)C(?)-D(?) Spin Pairs as a Probe of Backbone Dynamics in Proteins.
J Phys Chem B. 2013 Jan 25;
Authors: Sun H, Long D, Brüschweiler R, Tugarinov V
Abstract
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Site-Directed Methyl Group Labeling as an NMR Probe of Structure and Dynamics in Supramolecular Protein Systems: Applications to the Proteasome and to the ClpP Protease
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Tomasz L. Religa, Amy M. Ruschak, Rina Rosenzweig and Lewis E. Kay
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja202259a/aop/images/medium/ja-2011-02259a_0002.gif
Journal of the American Chemical Society
DOI: 10.1021/ja202259a
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/rQfCMlQFoW8
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Site-Directed Methyl Group Labeling as an NMR Probe of Structure and Dynamics in Supra-Molecular Protein Systems: Applications to the Proteasome and to the ClpP Protease.
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Site-Directed Methyl Group Labeling as an NMR Probe of Structure and Dynamics in Supra-Molecular Protein Systems: Applications to the Proteasome and to the ClpP Protease.
J Am Chem Soc. 2011 May 11;
Authors: Religa TL, Ruschak AM, Rosenzweig R, Kay LE
Methyl groups are powerful reporters of structure, motion and function in NMR studies of supra-molecular protein assemblies. Their...
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Structure, Dynamics, and Kinetics of Weak Protein-Protein Complexes from NMR Spin Relaxation Measurements of Titrated Solutions.
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Angew Chem Int Ed Engl. 2011 Mar 18;
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[NMR paper] A comparison of 15N NMR relaxation measurements with a molecular dynamics simulation:
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Proteins. 1993 Dec;17(4):375-90
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