Abstract
Membrane proteins perform numerous physiological functions that are critical for human health. DEER (Double Electron Electron Resonance) spectroscopy is playing an increasingly important role in characterizing the conformational states of these proteins. DEER is a powerful-pulsed EPR technique allowing the determination of spin-spin distance histograms between site-directed nitroxide label sites on a protein. Combining the DEER structural data with molecular dynamics (MD) simulation methods can be a powerful strategy to study membrane protein structure and function.
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