Abstract
Site-directed spin labeling (SDSL) in combination with electron paramagnetic resonance (EPR) spectroscopy is a rapidly expanding powerful biophysical technique to study the structural and dynamic properties of membrane proteins in a native environment. Membrane proteins are responsible for performing important functions in a wide variety of complicated biological systems that are responsible for the survival of living organisms. In this review, a brief introduction of the most popular SDSL EPR techniques and illustrations of recent applications for studying pertinent structural and dynamic properties on membrane proteins will be discussed.
Highlights
Molecular biology techniques have been developed to incorporate stable radicals at specific locations on biological systems extending the application of electron paramagnetic resonance (EPR) spectroscopy to nearly any biological system
continuous wave- (CW-)EPR lineshape analysis was performed on 53 sites of spin labeled KCNE1 including all 27 residues of the transmembrane domain (45–71), and 26 residues of the Nand C-termini of KCNE1 in lipid bilayered vesicles to study the nitroxide side-chain motion
The results indicated that the nitroxide spin label side-chains located in the KCNE1 transmembrane domain (TMD) are less mobile when compared to the extracellular region of KCNE1
Summary
This interaction is called the hyperfine interaction (A) and depends on the amount of electron spin density on the nucleus, the distance between the electron spin and the nucleus, and the angle between the two with respect to the magnetic field (B0) This hyperfine interaction produces a small change in the allowed energy levels of the electrons and splits the EPR lines into multiple lines depending on the nuclear spin state. X-ray crystallography and nuclear magnetic resonance (NMR) spectroscopy are the two most successful and popular biophysical techniques used to probe structural information on protein systems. EPR spectroscopy is a rapidly expanding and powerful biophysical technique to resolve these challenges and provides prominent solutions to glean structural and dynamic information on peptides, proteins, macromolecules, and nucleic acids [3, 8, 12, 17, 21,22,23, 47,48,49,50]
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