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Abstract
The fact that membrane proteins are notoriously difficult to analyse using standard protocols for atomic-resolution structure determination methods have motivated adaptation of these techniques to membrane protein studies as well as development of new technologies. With this motivation, liquid-state nuclear magnetic resonance (NMR) has recently been used with success for studies of peptides and membrane proteins in detergent micelles, and solid-state NMR has undergone a tremendous evolution towards characterization of membrane proteins in native membrane and oriented phospholipid bilayers. In this mini-review, we describe some of the technological challenges behind these efforts and provide examples on their use in membrane biology.
NMR, nuclear magnetic resonance; MAS, magic angle spinning; XRD, X-ray diffraction; AFM, atomic forace microscopy; EM, electron microscopy; MD, molecular dynamics; SDS, sodium dodecyl sulfate; PDB, Protein Data Bank; DMPC, dimyristoylphosphatidylcholine; bR, bacteriorhodopsin; GPCR, G-protein coupled receptor
NMR, nuclear magnetic resonance; MAS, magic angle spinning; XRD, X-ray diffraction; AFM, atomic forace microscopy; EM, electron microscopy; MD, molecular dynamics; SDS, sodium dodecyl sulfate; PDB, Protein Data Bank; DMPC, dimyristoylphosphatidylcholine; bR, bacteriorhodopsin; GPCR, G-protein coupled receptor