Membrane Proteins: Structure, Function and Motion

doi:10.3390/books978-3-0365-6538-5

Reprint

Download Flyer

Membrane Proteins: Structure, Function and Motion

Edited by

February 2023

516 pages

ISBN978-3-0365-6537-8 (Hardback)
ISBN978-3-0365-6538-5 (PDF)

https://0-doi-org.brum.beds.ac.uk/10.3390/books978-3-0365-6538-5

Free download (PDF)

This book is a reprint of the Special Issue Membrane Proteins: Structure, Function and Motion that was published in

Biology & Life Sciences

Chemistry & Materials Science

Medicine & Pharmacology

Summary

Membrane proteins are essential for the diverse biological functions of the cells and intercellular communication in living organisms. With the recent developments in the methodologies, the research on membrane proteins has been undergoing a major transformation. In this informative book, the biological and dynamic behaviour of membrane proteins are introduced, discussed, and reviewed by some of the leading researchers in the field. The main objective of this compendium is to present the recent research in the fundamental and advanced concepts and methodologies used for studying membrane proteins. Membrane protein purification and reconstitution, protein–lipid interaction, ion/substrate transport, conformational and functional dynamics, the interaction of infectious agents, cell death, and organelle morphology are among the topics that are covered. This reprint is intended for a broad range of novice and experienced scientists with different levels of experience, from biophysicists and biochemists to microbiologists, cell biologists, and physiologists.

Format

Hardback

License

Keywords

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