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Default Mapping Membrane Protein Backbone Dynamics: A Comparison of Site-Directed Spin Labeling with NMR (15)N-Relaxation Measurements.

Mapping Membrane Protein Backbone Dynamics: A Comparison of Site-Directed Spin Labeling with NMR (15)N-Relaxation Measurements.

Related Articles Mapping 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]



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