Outer membrane protein A of E. coli folds into detergent micelles, but not in the presence of monomeric detergent
about
Structure of outer membrane protein G by solution NMR spectroscopy.Oligomeric lipoprotein PelC guides Pel polysaccharide export across the outer membrane of Pseudomonas aeruginosa.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 foldingCysteine residues impact the stability and micelle interaction dynamics of the human mitochondrial β-barrel anion channel hVDAC-2Influence of protein-micelle ratios and cysteine residues on the kinetic stability and unfolding rates of human mitochondrial VDAC-2An engineered dimeric protein pore that spans adjacent lipid bilayers.Folding and stability of outer membrane protein A (OmpA) from Escherichia coli in an amphipathic polymer, amphipol A8-35.Lipid and membrane mimetic environments modulate spin label side chain configuration in the outer membrane protein A.The soluble, periplasmic domain of OmpA folds as an independent unit and displays chaperone activity by reducing the self-association propensity of the unfolded OmpA transmembrane β-barrel.The prediction and characterization of YshA, an unknown outer-membrane protein from Salmonella typhimurium.Solubilization and characterization of the anthrax toxin pore in detergent micellesOne membrane protein, two structures and six environments: a comparative molecular dynamics simulation study of the bacterial outer membrane protein PagP.The cavity-chaperone Skp protects its substrate from aggregation but allows independent folding of substrate domainsMicroscale NMR screening of new detergents for membrane protein structural biology.Refolding of Escherichia coli outer membrane protein F in detergent creates LPS-free trimers and asymmetric dimersSpontaneous formation of detergent micelles around the outer membrane protein OmpX.NMR solution structure determination of membrane proteins reconstituted in detergent micelles.Folding and insertion of the outer membrane protein OmpA is assisted by the chaperone Skp and by lipopolysaccharide.Lipid-protein interactions in DHPC micelles containing the integral membrane protein OmpX investigated by NMR spectroscopy.Structure and assembly of beta-barrel membrane proteins.Refolded outer membrane protein A of Escherichia coli forms ion channels with two conductance states in planar lipid bilayers.Structural transitions in short-chain lipid assemblies studied by (31)P-NMR spectroscopyStructure, dynamics and function of the outer membrane protein A (OmpA) and influenza hemagglutinin fusion domain in detergent micelles by solution NMR.Mycobacterium tuberculosis chaperonin 10 is secreted in the macrophage phagosome: is secretion due to dissociation and adoption of a partially helical structure at the membrane?Conformation of gramicidin A in Triton X-100 micelles from CD and FTIR data: a clean example of antiparallel double β5.6 helix formation.Detergent binding explains anomalous SDS-PAGE migration of membrane proteins.Unfolding free energy of a two-domain transmembrane sugar transport protein.Self-association of unfolded outer membrane proteins.Effects of urea on the microstructure and phase behavior of aqueous solutions of polyoxyethylene surfactants.Overcoming hysteresis to attain reversible equilibrium folding for outer membrane phospholipase A in phospholipid bilayers.Interactions between folding factors and bacterial outer membrane proteins.A novel mechanism of "metal gel-shift" by histidine-rich Ni2+-binding Hpn protein from Helicobacter pylori strain SS1.Expression, refolding, crystallization and preliminary X-ray analysis of Pseudomonas aeruginosa AlgE.Membrane proteins structure and dynamics by nuclear magnetic resonance.The protein pheromone temptin is an attractant of the gastropod Biomphalaria glabrata.Outer membrane protein A of bovine and ovine isolates of Mannheimia haemolytica is surface exposed and contains host species-specific epitopesResolving the native conformation of Escherichia coli OmpA.Surface-accessible residues in the monomeric and assembled forms of a bacterial surface layer protein.Liprotides assist in folding of outer membrane proteins.
P2860
Q27648701-8A73A9EC-51FE-4BB9-8C6C-474DEC2C935AQ30152656-DF4ED592-3125-408F-B057-2CD44B91B601Q30153331-3AEDE6CE-0EC2-46D7-B98B-C05AE0DE229CQ30153375-6C5DBF0A-89E5-4F99-82BA-3033160D1F5DQ30153423-219AEC8D-2DEB-4FC2-8665-087C86389873Q30153438-08BE0B45-2EFA-430F-94C9-B8BC6E12F802Q30155111-F5900B82-5CA2-4E6C-9683-6FFB33A110EBQ30155140-4268AA46-F7C9-4238-B8A1-5B8A3450CA47Q30155443-AC0B739B-5E77-405E-AFFC-EB80060352E2Q30155509-BFA7986F-176F-4159-A8B2-942573711CA5Q30156014-B388B953-7F36-43AC-9DF5-3BE950BB1A87Q30157192-B3496972-B0FC-4499-A3AF-C51832639618Q30157331-A3FF568C-0044-4EB6-B7DA-B71D65C62349Q30157376-AE44AFCD-CB12-4483-A5A2-E5BF72384D9EQ30157675-0BDD95DA-D825-4E5B-8C3B-92161B46FDD3Q30160137-785397F4-E4E9-4DAE-9C98-16EDDA0366DCQ30160297-1C704E59-41F3-424D-81C6-8441517FAC64Q30164395-A5B05521-9A0B-434B-9374-0958334980C2Q30164981-B81229A6-D803-440C-99A2-F62B76523B24Q30165158-322DEC0A-12B1-45E2-A4F3-6058A562F1E3Q30168071-0DB985BD-2A10-4B66-A074-B95E00B0E352Q30175269-8F0E7497-7973-4AE3-96BE-732740D15536Q30309646-26429205-4D6C-4854-AD1C-70D1B5717A79Q30311962-ED22BD10-A607-4025-96DE-86BCC8FB60A5Q30333133-6B6B37DD-A84B-4082-8EF2-23382BDF9471Q30634414-D02F3F9D-A89A-4A63-B57E-FB7BAA80CCEEQ33404282-C80FA180-A770-42F2-8ED4-7CEAED1CB3D4Q34276447-8277ACC6-22C8-42D1-BE59-66C0B60A64DCQ34513200-3580E718-F43A-466F-81EC-D29926BDAF26Q34606674-0C061C6A-FC86-4B92-80A3-98598665A494Q35349779-DAB3AE7B-EA8D-4B9A-88CC-96A61A3D6687Q36174616-EE8A1378-CDBF-4D8F-ADCB-4983320B4AB0Q36282913-F4FF8D1A-B3D4-4511-B5A8-8CDCA650CB6FQ37175296-4B9D65CD-564A-4B82-99A1-2A3A29173899Q38111739-C8264251-3360-4978-88FA-953A5E309BADQ39356136-6A26463B-5A79-479B-A828-627762BFAB07Q40387690-9864D91B-37BD-4050-9E9C-CF3A32BEADE9Q42699659-BBAB0B86-60B1-4B81-9BD8-115973A11B93Q43027905-848B333B-5612-4FC7-A7C5-19ECA9A809F8Q48378148-20D97C3F-FF2B-4499-A732-7AD57F60D571
P2860
Outer membrane protein A of E. coli folds into detergent micelles, but not in the presence of monomeric detergent
description
1999 nî lūn-bûn
@nan
1999 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Outer membrane protein A of E. ...... resence of monomeric detergent
@ast
Outer membrane protein A of E. ...... resence of monomeric detergent
@en
type
label
Outer membrane protein A of E. ...... resence of monomeric detergent
@ast
Outer membrane protein A of E. ...... resence of monomeric detergent
@en
prefLabel
Outer membrane protein A of E. ...... resence of monomeric detergent
@ast
Outer membrane protein A of E. ...... resence of monomeric detergent
@en
P2093
P2860
P921
P356
P1433
P1476
Outer membrane protein A of E. ...... resence of monomeric detergent
@en
P2093
J H Kleinschmidt
M C Wiener
P2860
P304
P356
10.1110/PS.8.10.2065
P577
1999-10-01T00:00:00Z