Electron Paramagnetic Resonance as a Tool for Studying Membrane Proteins

Biomolecules. 2020 May 13;10(5):763. doi: 10.3390/biom10050763.

Abstract

Membrane proteins possess a variety of functions essential to the survival of organisms. However, due to their inherent hydrophobic nature, it is extremely difficult to probe the structure and dynamic properties of membrane proteins using traditional biophysical techniques, particularly in their native environments. Electron paramagnetic resonance (EPR) spectroscopy in combination with site-directed spin labeling (SDSL) is a very powerful and rapidly growing biophysical technique to study pertinent structural and dynamic properties of membrane proteins with no size restrictions. In this review, we will briefly discuss the most commonly used EPR techniques and their recent applications for answering structure and conformational dynamics related questions of important membrane protein systems.

Keywords: Membrane protein; double electron electron resonance (DEER); electron paramagnetic resonance (EPR), site-directed spin labeling; membrane mimetic; structural and dynamics.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Review

MeSH terms

  • Animals
  • Electron Spin Resonance Spectroscopy / methods
  • Humans
  • Membrane Proteins / chemistry*
  • Nuclear Magnetic Resonance, Biomolecular / methods*
  • Spin Trapping / methods

Substances

  • Membrane Proteins