Abstract
Membrane proteins are essential for the survival of living organisms. They are involved in important biological functions including transportation of ions and molecules across the cell membrane and triggering the signaling pathways. They are targets of more than half of the modern medical drugs. Despite their biological significance, information about the structural dynamics of membrane proteins is lagging when compared to that of globular proteins. The major challenges with these systems are low expression yields and lack of appropriate solubilizing medium required for biophysical techniques. Electron paramagnetic resonance (EPR) spectroscopy coupled with site directed spin labeling (SDSL) is a rapidly growing powerful biophysical technique that can be used to obtain pertinent structural and dynamic information on membrane proteins. In this brief review, we will focus on the overview of the widely used EPR approaches and their emerging applications to answer structural and conformational dynamics related questions on important membrane protein systems.
Highlights
Membrane ProteinsMembrane proteins are very important biological systems responsible for biological functions vital to the survival of living organisms [1,2]
Membrane proteins are essential for the survival of living organisms
Authors further concluded that the styrene maleic acid lipid nanoparticles (SMALPs) could be suitable for the preparation of stable and functional membrane protein samples for spectroscopic studies of their conformation and dynamics with possible restrictions of conformational changes in the transmembrane region of proteins [145]
Summary
Membrane proteins are very important biological systems responsible for biological functions vital to the survival of living organisms [1,2]. Available and widely used membrane mimetic systems are detergent micelles, bicelles, liposomes, lipodiscs, and lipodisq nanoparticles/SMALPs (styrene maleic acid lipid particles) [12,13,14,15,16]. These membrane mimetic systems have their own benefits and limitations. The use of nanodisc as membrane mimetic systems has been very popular recently in biophysical studies of membrane protein with the benefit of no restriction on the types of lipids that can be used [17,18,19] This system utilizes membrane scaffold protein as a solubilizing unit which may potentially affect the optical studies of the target protein.
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