Forces and factors that contribute to the structural stability of membrane proteins.
about
Quantification of helix-helix binding affinities in micelles and lipid bilayersIdentification of native atrial G-protein-regulated inwardly rectifying K+ (GIRK4) channel homomultimersInactivation mechanism of the membrane protein diacylglycerol kinase in detergent solutionMethionine mutations of outer membrane protein X influence structural stability and beta-barrel unfoldingA Supercomplex Spanning the Inner and Outer Membranes Mediates the Biogenesis of β-Barrel Outer Membrane Proteins in Bacteria.Differential contribution of tryptophans to the folding and stability of the attachment invasion locus transmembrane β-barrel from Yersinia pestis.Kinetics and thermodynamics of membrane protein foldingInfluence of protein-micelle ratios and cysteine residues on the kinetic stability and unfolding rates of human mitochondrial VDAC-2Engineered oligomerization state of OmpF protein through computational design decouples oligomer dissociation from unfolding.Improving the resistance of a eukaryotic β-barrel protein to thermal and chemical perturbations.Predicting weakly stable regions, oligomerization state, and protein-protein interfaces in transmembrane domains of outer membrane proteins.Thermodynamics of unfolding of an integral membrane protein in mixed micelles.Analysis of the structural organization and thermal stability of two spermadhesins. Calorimetric, circular dichroic and Fourier-transform infrared spectroscopic studies.Probing the binding site of 800-nm bacteriochlorophyll in the membrane-linked LH2 protein of Rhodobacter capsulatus by local unfolding and chemical modification: evidence for the involvement of a betaHis20 residue.Elastic coupling of integral membrane protein stability to lipid bilayer forces.Geometry and intrinsic tilt of a tryptophan-anchored transmembrane alpha-helix determined by (2)H NMRComparison of the dynamics of the primary events of bacteriorhodopsin in its trimeric and monomeric states.Helical distortion in tryptophan- and lysine-anchored membrane-spanning alpha-helices as a function of hydrophobic mismatch: a solid-state deuterium NMR investigation using the geometric analysis of labeled alanines methodTRPV1 temperature activation is specifically sensitive to strong decreases in amino acid hydrophobicity.Thermally induced aggregation of human transferrin receptor studied by light-scattering techniquesCross-linking of cell surface receptors enhances cooperativity of molecular adhesionSpectroscopic analysis of halothane binding to the plasma membrane Ca2+-ATPase.Use of thiol-disulfide equilibria to measure the energetics of assembly of transmembrane helices in phospholipid bilayers.Differential scanning calorimetry: An invaluable tool for a detailed thermodynamic characterization of macromolecules and their interactionsPredicting the complex structure and functional motions of the outer membrane transporter and signal transducer FecA.Thermal unfolding of a mammalian pentameric ligand-gated ion channel proceeds at consecutive, distinct stepsDelipidation of cytochrome c oxidase from Rhodobacter sphaeroides destabilizes its quaternary structure.Application of the Wang-Landau algorithm to the dimerization of glycophorin A.Sequential dissociation of subunits from bovine heart cytochrome C oxidase by urea.Introduction to membrane proteins.Mechanistic studies of the biogenesis and folding of outer membrane proteins in vitro and in vivo: what have we learned to date?Role of the transmembrane domain in the stability of TrwB, an integral protein involved in bacterial conjugation.A surface-exposed region of a novel outer membrane protein (P66) of Borrelia spp. is variable in size and sequence.Unfolding pathways of native bacteriorhodopsin depend on temperature.Putative interhelical interactions within the PheP protein revealed by second-site suppressor analysis.Stability of bacteriorhodopsin alpha-helices and loops analyzed by single-molecule force spectroscopy.Modeling of the three-dimensional structure of the digitalis intercalating matrix in Na+/K(+)-ATPase protodimer.ATP synthesis catalyzed by a V-ATPase: an alternative pathway for energy conservation operating in plant vacuoles?Analysis of adenosine A₂a receptor stability: effects of ligands and disulfide bonds.Evidence for phospholipid microdomain formation in liquid crystalline liposomes reconstituted with Escherichia coli lactose permease.
P2860
Q24645279-6A3D744A-7E30-4493-B501-A6A6DDCF04F8Q28284897-20F1AE2A-F3EE-491F-9854-DF8F8A8B3731Q28361373-6EBDA564-10E4-4ACB-90D6-CA5FD4C809B6Q28535036-6F7F2ACA-0F9C-4637-96FF-D9DCB7E51B46Q30152772-7B2F60B2-D925-4F30-99C8-7712C7F1F67CQ30153331-9B381D8D-387F-428A-87BD-F8B16772289EQ30153375-AA839038-A19C-414E-9D43-F2281DCA66F2Q30153438-3056CF04-A2A3-4DDA-A5B0-349FD90A752FQ30155362-33FF9540-DD73-4754-90DE-CE795B0EA6AEQ30155492-8A593226-0A20-40F0-8DA0-B7E530E2D700Q30157187-051DCF1D-D4B7-4BCC-BD8A-02EE89B1B035Q30159843-E8AE3384-962B-4FF8-A199-9701B0E50F37Q30192826-CE17D2DB-442A-4A6C-BBE8-699AAD9C9D3BQ30328223-49BCF2F3-621A-4D99-8657-571C16E939E6Q30433035-71F83A50-8569-4B9A-9136-5E21F26CB6D4Q30717237-029FB1C9-13B4-4702-9A26-4D7AE787754AQ31105953-AF4D235F-B4D5-4466-8995-65D84417BF18Q31126703-A850EBDB-E0E7-4AA3-AC5F-EC6027FD51E2Q33674257-593CD2C1-311D-4C50-9EC9-E08F32036E7EQ34171154-0CC79BF9-37D4-46BD-8981-68EE526F9E1AQ34173183-3866020B-5724-42CF-959B-60923A7ADAC6Q34179980-CC91E96F-866B-408E-87B2-FFE13E6BD583Q34385274-5116FF7F-1E24-4420-8A6E-A432F69BC942Q34648464-0F32C2F1-7C6D-4F17-9266-29B63233B5FFQ36494863-9CB37282-AB75-404A-ADB5-B14022D9C64DQ36636020-2CDC565F-520C-45FF-BF35-8020A5720CC3Q36901556-77BA0BDF-D9F8-4A6C-8C1F-1F049127C763Q37285429-8D161DA3-63F6-484A-A43F-BCCAC478A6AAQ37350753-F806AD62-371A-4677-96D9-397B68872608Q37980398-69314BB7-9075-4A80-B1E0-2ADC781A690EQ38194733-C75630D0-82D5-4094-88B0-9082769D59C8Q38346461-ABB145FA-34A9-4873-93D8-8E255D6E9098Q39565174-D60B1031-0869-4F27-96B8-90B89E314EE1Q39927873-CBDC7FFD-B788-4A4D-B6F1-352B23FB3259Q39981841-B9DE27EF-C29A-4EE9-97FB-F3A5A1EAB414Q40220193-A301102F-75F6-4D3A-B8BC-B5BDE9DC0EFDQ41135295-FB31EEB9-86C8-4C53-97D3-E267379D3071Q41959752-19B3B3EF-C433-4B8B-A06A-8770146C8102Q41988339-0494F9DF-691D-4EEB-9DA9-935DDD9CB4C4Q42029598-22893F2E-2CBA-4292-B1ED-4BB543005A07
P2860
Forces and factors that contribute to the structural stability of membrane proteins.
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
1995年论文
@zh
1995年论文
@zh-cn
name
Forces and factors that contribute to the structural stability of membrane proteins.
@en
type
label
Forces and factors that contribute to the structural stability of membrane proteins.
@en
prefLabel
Forces and factors that contribute to the structural stability of membrane proteins.
@en
P1476
Forces and factors that contribute to the structural stability of membrane proteins.
@en
P2093
P356
10.1016/0005-2728(94)00161-W
P577
1995-02-01T00:00:00Z