Journal
MEMBRANES
Volume 12, Issue 2, Pages -Publisher
MDPI
DOI: 10.3390/membranes12020227
Keywords
membrane proteins; membrane protein structure; membrane protein dynamics; NMR; cryo-EM; X-ray; FRET; EPR; HDX-MS; antibody fragments
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This review discusses various techniques used in studying protein dynamics, including NMR, cryo-EM, and X-ray crystallography, as well as methods for conformational trapping using specific binders. It also showcases the application of biophysical techniques such as FRET, EPR, and computational approaches in GPCRs, transporters, and ion channels.
A plethora of membrane proteins are found along the cell surface and on the convoluted labyrinth of membranes surrounding organelles. Since the advent of various structural biology techniques, a sub-population of these proteins has become accessible to investigation at near-atomic resolutions. The predominant bona fide methods for structure solution, X-ray crystallography and cryo-EM, provide high resolution in three-dimensional space at the cost of neglecting protein motions through time. Though structures provide various rigid snapshots, only an amorphous mechanistic understanding can be inferred from interpolations between these different static states. In this review, we discuss various techniques that have been utilized in observing dynamic conformational intermediaries that remain elusive from rigid structures. More specifically we discuss the application of structural techniques such as NMR, cryo-EM and X-ray crystallography in studying protein dynamics along with complementation by conformational trapping by specific binders such as antibodies. We finally showcase the strength of various biophysical techniques including FRET, EPR and computational approaches using a multitude of succinct examples from GPCRs, transporters and ion channels.
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