期刊
BIOCHEMISTRY
卷 52, 期 38, 页码 6627-6632出版社
AMER CHEMICAL SOC
DOI: 10.1021/bi4009984
关键词
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资金
- National Institutes of Health [R01 GM108026, R01 GM080542, R01 DC007416]
- National Science Foundation (NSF) [CHE-1011909]
- NSF
- Ohio Board of Regents grants [MRI-0722403]
- Division Of Chemistry
- Direct For Mathematical & Physical Scien [1305664] Funding Source: National Science Foundation
- Division Of Chemistry
- Direct For Mathematical & Physical Scien [1011909] Funding Source: National Science Foundation
Pulsed EPR DEER structural studies of membrane proteins in a lipid bilayer have often been hindered by difficulties in extracting accurate distances when compared to those of globular proteins. In this study, we employed a combination of three recently developed methodologies, (1) bifunctional spin labels (BSL), (2) SMA-Lipodisq nanoparticles, and (3) Q band pulsed EPR measurements, to obtain improved signal sensitivity, increased transverse relaxation time, and more accurate and precise distances in DEER measurements on the integral membrane protein KCNE1. The KCNE1 EPR data indicated an similar to 2-fold increase in the transverse relaxation time for the SMA-Lipoclisq nanoparticles when compared to those of proteoliposomes and narrower distance distributions for the BSL when compared to those of the standard MTSL. The certainty of information content in DEER data obtained for KCNE1 in SMA-Lipodisq nanoparticles is comparable to that in micelles. The combination of techniques will enable researchers to potentially obtain more precise distances in cases where the traditional spin labels and membrane systems yield imprecise distance distributions.
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