Membrane Proteins: Structure, Function and Motion

© 2022 by the authors; CC BY-NC-ND license

band 3; red blood cells; antimalarial drugs; molecular docking; molecular dynamics; membrane mechanics; molecular dynamics; flicker-noise spectroscopy; neurodegeneration; amyloid-beta peptides; pressure wave; giant unilamellar vesicles; membrane protein; lipid bilayer; membrane mimetic; potassium channels; tetraalkylammonium salts; protein thermal stability; homo-FRET; C-type inactivation; binding affinity; selectivity filter conformation; steady-state and time-resolved fluorescence anisotropy; membrane protein; long-chain fatty acid; proton transfer; purine nucleotide; conductance measurements in model membranes; uncoupling; SARS-CoV-2; Betacoronavirus; Coronaviridae; transmembrane proteins; pathogenesis; inflammation; immunity; vaccines; CA3-CA1 synapses; NMDA; AMPA; systems biology; multiscale modeling; Schaffer collateral-CA1 synapses; fatty acid anion transport; proton transport; ADP/ATP carrier protein; mitochondrial transporter; arachidonic acid; long-chain fatty acids; nitric oxide; ferroptosis; lipid peroxidation; lipoxygenase structure; O₂ and NO^● binding mechanisms; 1-stearoyl-2-arachidonoyl phosphatidylethanolamine (1-SA-2-ETE-PE or SAPE); lipidomics; MD simulations; influenza virus fusion peptides; peptide-membrane interactions; membrane fusion; membrane; peptidoglycan; efflux pump assembly; resistance; Pseudomonas; AAA-type protease; Arabidopsis thaliana; FtsH metalloprotease; chloroplast; embryo lethal; leaf variegation; plastid biogenesis; protein import; oxidative stress; membrane protein; lipid–protein interaction; cryo-electron microscopy; hydrogen–deuterium exchange mass spectrometry; native mass spectrometry; single-molecule Förster resonance energy transfer; double electron–electron resonance; native mass spectrometry; angulin-1; LSR; tricellulin; tricellular tight junction; paracellular water transport; tight epithelium; MDCK C7 cells; intermediate-tight epithelium; HT-29/B6 cells; apoptosis; mitochondria; Bcl-2 family; Bax; Bid; membrane protein; protein–protein interaction; protein oligomerization; fluorescence; single particle detection; tetraspanins; CD81; CD82; gangliosides; single-molecule tracking; microdomain; membrane diffusion; fluorescence microscopy; integral membrane protein; membrane lipid; structure; function; oligomeric state; cryo-EM; advanced mass spectrometry; molecular dynamics; membrane mimetic systems; HMG-CoA reductase; HMGR; HMGR vesicle; ER-HMGR domain; mevalonate; endoplasmic reticulum; OSER; high-pressure freezing; chemical fixation; Archaerhodopsin-3; lipid bilayer; microfluidics; cell-free gene expression; cytochrome b₅ reductase; cytochrome b₅; superoxide anion radical; electron transfer; protein intrinsic dynamics; odorant receptor; chemosensory; membrane traffic; heterologous expression; mitochondrial carriers; uncoupling proteins; ADP/ATP carrier; membrane protein structure and function; regulation and mechanism of proton transport; membrane protein oligomerization; ATP synthesis; biphasic proton transport model; alternating access mechanism; reactive oxygen species control; chloroplast-targeting pathways; chloroplast outer membrane proteome; signal anchored protein; tail anchored protein; β-barrel protein; β-signal; chloroplast transit peptide; TOC complex; AKR2; OEP80; ATP-binding cassette (ABC) transporter; multidrug and toxic compound extrusion (MATE) transporter; monosaccharide transporter (MST); sucrose transporter (SUT); amino acid transporter; detoxification; nutrient transport; stress adaptation; proton gradient; cellular pH; small HSP; lipid–protein interaction; membrane chaperone; membrane fluidity; stress response; n/a