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Biophys J. 2014 Oct 7;107(7):1697-702. doi: 10.1016/j.bpj.2014.08.018.

Mapping membrane protein backbone dynamics: a comparison of site-directed spin labeling with NMR 15N-relaxation measurements.

Author information

1
Department of Chemistry, University of Virginia, Charlottesville, Virginia.
2
Department of Chemistry, University of Virginia, Charlottesville, Virginia. Electronic address: columbus@virginia.edu.

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
PMCID:
PMC4190660
DOI:
10.1016/j.bpj.2014.08.018
[Indexed for MEDLINE]
Free PMC Article

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