Journal
STRUCTURE
Volume 19, Issue 11, Pages 1549-1561Publisher
CELL PRESS
DOI: 10.1016/j.str.2011.10.009
Keywords
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Funding
- National Institutes of Health [U54 GM087519, R01 GM077659]
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Trapping membrane proteins in the confines of a crystal lattice obscures dynamic modes essential for inter-conversion between multiple conformations in the functional cycle. Moreover, lattice forces could conspire with detergent solubilization to stabilize a minor conformer in an ensemble thus confounding mechanistic interpretation. Spin labeling in conjunction with electron paramagnetic resonance (EPR) spectroscopy offers an exquisite window into membrane protein dynamics in the native-like environment of a lipid bilayer. Systematic application of spin labeling and EPR identifies sequence-specific secondary structures, defines their topology and their packing in the tertiary fold. Long range distance measurements (60 angstrom-80 angstrom) between pairs of spin labels enable quantitative analysis of equilibrium dynamics and triggered conformational changes. This review highlights the contribution of spin labeling to bridging structure and mechanism. Efforts to develop methods for determining structures from EPR restraints and to increase sensitivity and throughput promise to expand spin labeling applications in membrane protein structural biology.
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