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dc.contributor.editorJelokhani-Niaraki, Masoud
dc.date.accessioned2023-04-05T12:49:15Z
dc.date.available2023-04-05T12:49:15Z
dc.date.issued2023
dc.identifierONIX_20230405_9783036565378_30
dc.identifier.urihttps://directory.doabooks.org/handle/20.500.12854/98751
dc.description.abstractMembrane 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.
dc.languageEnglish
dc.subject.classificationthema EDItEUR::G Reference, Information and Interdisciplinary subjects::GP Research and information: generalen_US
dc.subject.classificationthema EDItEUR::P Mathematics and Science::PS Biology, life sciencesen_US
dc.subject.otherband 3
dc.subject.otherred blood cells
dc.subject.otherantimalarial drugs
dc.subject.othermolecular docking
dc.subject.othermolecular dynamics
dc.subject.othermembrane mechanics
dc.subject.otherflicker-noise spectroscopy
dc.subject.otherneurodegeneration
dc.subject.otheramyloid-beta peptides
dc.subject.otherpressure wave
dc.subject.othergiant unilamellar vesicles
dc.subject.othermembrane protein
dc.subject.otherlipid bilayer
dc.subject.othermembrane mimetic
dc.subject.otherpotassium channels
dc.subject.othertetraalkylammonium salts
dc.subject.otherprotein thermal stability
dc.subject.otherhomo-FRET
dc.subject.otherC-type inactivation
dc.subject.otherbinding affinity
dc.subject.otherselectivity filter conformation
dc.subject.othersteady-state and time-resolved fluorescence anisotropy
dc.subject.otherlong-chain fatty acid
dc.subject.otherproton transfer
dc.subject.otherpurine nucleotide
dc.subject.otherconductance measurements in model membranes
dc.subject.otheruncoupling
dc.subject.otherSARS-CoV-2
dc.subject.otherBetacoronavirus
dc.subject.otherCoronaviridae
dc.subject.othertransmembrane proteins
dc.subject.otherpathogenesis
dc.subject.otherinflammation
dc.subject.otherimmunity
dc.subject.othervaccines
dc.subject.otherCA3-CA1 synapses
dc.subject.otherNMDA
dc.subject.otherAMPA
dc.subject.othersystems biology
dc.subject.othermultiscale modeling
dc.subject.otherSchaffer collateral-CA1 synapses
dc.subject.otherfatty acid anion transport
dc.subject.otherproton transport
dc.subject.otherADP/ATP carrier protein
dc.subject.othermitochondrial transporter
dc.subject.otherarachidonic acid
dc.subject.otherlong-chain fatty acids
dc.subject.othernitric oxide
dc.subject.otherferroptosis
dc.subject.otherlipid peroxidation
dc.subject.otherlipoxygenase structure
dc.subject.otherO2 and NO● binding mechanisms
dc.subject.other1-stearoyl-2-arachidonoyl phosphatidylethanolamine (1-SA-2-ETE-PE or SAPE)
dc.subject.otherlipidomics
dc.subject.otherMD simulations
dc.subject.otherinfluenza virus fusion peptides
dc.subject.otherpeptide-membrane interactions
dc.subject.othermembrane fusion
dc.subject.othermembrane
dc.subject.otherpeptidoglycan
dc.subject.otherefflux pump assembly
dc.subject.otherresistance
dc.subject.otherPseudomonas
dc.subject.otherAAA-type protease
dc.subject.otherArabidopsis thaliana
dc.subject.otherFtsH metalloprotease
dc.subject.otherchloroplast
dc.subject.otherembryo lethal
dc.subject.otherleaf variegation
dc.subject.otherplastid biogenesis
dc.subject.otherprotein import
dc.subject.otheroxidative stress
dc.subject.otherlipid–protein interaction
dc.subject.othercryo-electron microscopy
dc.subject.otherhydrogen–deuterium exchange mass spectrometry
dc.subject.othernative mass spectrometry
dc.subject.othersingle-molecule Förster resonance energy transfer
dc.subject.otherdouble electron–electron resonance
dc.subject.otherangulin-1
dc.subject.otherLSR
dc.subject.othertricellulin
dc.subject.othertricellular tight junction
dc.subject.otherparacellular water transport
dc.subject.othertight epithelium
dc.subject.otherMDCK C7 cells
dc.subject.otherintermediate-tight epithelium
dc.subject.otherHT-29/B6 cells
dc.subject.otherapoptosis
dc.subject.othermitochondria
dc.subject.otherBcl-2 family
dc.subject.otherBax
dc.subject.otherBid
dc.subject.otherprotein–protein interaction
dc.subject.otherprotein oligomerization
dc.subject.otherfluorescence
dc.subject.othersingle particle detection
dc.subject.othertetraspanins
dc.subject.otherCD81
dc.subject.otherCD82
dc.subject.othergangliosides
dc.subject.othersingle-molecule tracking
dc.subject.othermicrodomain
dc.subject.othermembrane diffusion
dc.subject.otherfluorescence microscopy
dc.subject.otherintegral membrane protein
dc.subject.othermembrane lipid
dc.subject.otherstructure
dc.subject.otherfunction
dc.subject.otheroligomeric state
dc.subject.othercryo-EM
dc.subject.otheradvanced mass spectrometry
dc.subject.othermembrane mimetic systems
dc.subject.otherHMG-CoA reductase
dc.subject.otherHMGR
dc.subject.otherHMGR vesicle
dc.subject.otherER-HMGR domain
dc.subject.othermevalonate
dc.subject.otherendoplasmic reticulum
dc.subject.otherOSER
dc.subject.otherhigh-pressure freezing
dc.subject.otherchemical fixation
dc.subject.otherArchaerhodopsin-3
dc.subject.othermicrofluidics
dc.subject.othercell-free gene expression
dc.subject.othercytochrome b5 reductase
dc.subject.othercytochrome b5
dc.subject.othersuperoxide anion radical
dc.subject.otherelectron transfer
dc.subject.otherprotein intrinsic dynamics
dc.subject.otherodorant receptor
dc.subject.otherchemosensory
dc.subject.othermembrane traffic
dc.subject.otherheterologous expression
dc.subject.othermitochondrial carriers
dc.subject.otheruncoupling proteins
dc.subject.otherADP/ATP carrier
dc.subject.othermembrane protein structure and function
dc.subject.otherregulation and mechanism of proton transport
dc.subject.othermembrane protein oligomerization
dc.subject.otherATP synthesis
dc.subject.otherbiphasic proton transport model
dc.subject.otheralternating access mechanism
dc.subject.otherreactive oxygen species control
dc.subject.otherchloroplast-targeting pathways
dc.subject.otherchloroplast outer membrane proteome
dc.subject.othersignal anchored protein
dc.subject.othertail anchored protein
dc.subject.otherβ-barrel protein
dc.subject.otherβ-signal
dc.subject.otherchloroplast transit peptide
dc.subject.otherTOC complex
dc.subject.otherAKR2
dc.subject.otherOEP80
dc.subject.otherATP-binding cassette (ABC) transporter
dc.subject.othermultidrug and toxic compound extrusion (MATE) transporter
dc.subject.othermonosaccharide transporter (MST)
dc.subject.othersucrose transporter (SUT)
dc.subject.otheramino acid transporter
dc.subject.otherdetoxification
dc.subject.othernutrient transport
dc.subject.otherstress adaptation
dc.subject.otherproton gradient
dc.subject.othercellular pH
dc.subject.othersmall HSP
dc.subject.othermembrane chaperone
dc.subject.othermembrane fluidity
dc.subject.otherstress response
dc.subject.othern/a
dc.titleMembrane Proteins: Structure, Function and Motion
dc.typebook
oapen.identifier.doi10.3390/books978-3-0365-6538-5
oapen.relation.isPublishedBy46cabcaa-dd94-4bfe-87b4-55023c1b36d0
oapen.relation.isbn9783036565378
oapen.relation.isbn9783036565385
oapen.pages516
oapen.place.publicationBasel


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