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Solution NMR: A powerful tool for structural and functional studies of membrane proteins in reconstituted environments

The Journal of biological chemistry, 2019-11, Vol.294 (44), p.15914-15931 [Peer Reviewed Journal]

2019 © 2019 Puthenveetil and Vinogradova. ;2019 Puthenveetil and Vinogradova. ;2019 Puthenveetil and Vinogradova. 2019 Puthenveetil and Vinogradova. ;ISSN: 0021-9258 ;EISSN: 1083-351X ;DOI: 10.1074/jbc.REV119.009178 ;PMID: 31551353

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  • Title:
    Solution NMR: A powerful tool for structural and functional studies of membrane proteins in reconstituted environments
  • Author: Puthenveetil, Robbins ; Vinogradova, Olga
  • Subjects: amphipol ; Animals ; bicelle ; G-protein–coupled receptor (GPCR) ; Humans ; JBC Reviews ; Lipid Bilayers - chemistry ; Magnetic Resonance Spectroscopy - methods ; membrane mimetic ; membrane protein ; Membrane Proteins - chemistry ; Membrane Proteins - metabolism ; micelle ; Micelles ; nanodisc ; Nanostructures - chemistry ; nanotechnology ; nuclear magnetic resonance (NMR) ; Protein Domains ; structural biology
  • Is Part Of: The Journal of biological chemistry, 2019-11, Vol.294 (44), p.15914-15931
  • Description: A third of the genes in prokaryotic and eukaryotic genomes encode membrane proteins that are either essential for signal transduction and solute transport or function as scaffold structures. Unlike many of their soluble counterparts, the overall structural and functional organization of membrane proteins is sparingly understood. Recent advances in X-ray crystallography, cryo-EM, and nuclear magnetic resonance (NMR) are closing this gap by enabling an in-depth view of these ever-elusive proteins at atomic resolution. Despite substantial technological advancements, however, the overall proportion of membrane protein entries in the Protein Data Bank (PDB) remains <4%. This paucity is mainly attributed to difficulties associated with their expression and purification, propensity to form large multisubunit complexes, and challenges pertinent to identification of an ideal detergent, lipid, or detergent/lipid mixture that closely mimic their native environment. NMR is a powerful technique to obtain atomic-resolution and dynamic details of a protein in solution. This is accomplished through an assortment of isotopic labeling schemes designed to acquire multiple spectra that facilitate deduction of the final protein structure. In this review, we discuss current approaches and technological developments in the determination of membrane protein structures by solution NMR and highlight recent structural and mechanistic insights gained with this technique. We also discuss strategies for overcoming size limitations in NMR applications, and we explore a plethora of membrane mimetics available for the structural and mechanistic understanding of these essential cellular proteins.
  • Publisher: United States: Elsevier Inc
  • Language: English
  • Identifier: ISSN: 0021-9258
    EISSN: 1083-351X
    DOI: 10.1074/jbc.REV119.009178
    PMID: 31551353
  • Source: Open Access: PubMed Central
    MEDLINE
    Alma/SFX Local Collection
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