Gauging a hydrocarbon ruler by an intrinsic exciton probe.
about
PagP Crystallized from SDS/Cosolvent Reveals the Route for Phospholipid Access to the Hydrocarbon RulerA thiolate anion buried within the hydrocarbon ruler perturbs PagP lipid acyl chain selectionInscribing the perimeter of the PagP hydrocarbon ruler by site-specific chemical alkylationNovel Kinetic Intermediates Populated along the Folding Pathway of the Transmembrane β-Barrel OmpA.Aqueous, Unfolded OmpA Forms Amyloid-Like Fibrils upon Self-Association.Amphipols outperform dodecylmaltoside micelles in stabilizing membrane protein structure in the gas phase.A divergent Pseudomonas aeruginosa palmitoyltransferase essential for cystic fibrosis-specific lipid A.Dissecting the effects of periplasmic chaperones on the in vitro folding of the outer membrane protein PagPAmphipathic polymers enable the study of functional membrane proteins in the gas phaseThe 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.Molecular mechanism for lateral lipid diffusion between the outer membrane external leaflet and a beta-barrel hydrocarbon rulerStructural biology of membrane-intrinsic beta-barrel enzymes: sentinels of the bacterial outer membraneThe N-terminal helix is a post-assembly clamp in the bacterial outer membrane protein PagP.Probing tertiary structure of proteins using single Trp mutations with circular dichroism at low temperature.Exciton circular dichroism couplet arising from nitrile-derivatized aromatic residues as a structural probe of proteins.A tyrosine-tryptophan dyad and radical-based charge transfer in a ribonucleotide reductase-inspired maquette.Systematic analysis of the use of amphipathic polymers for studies of outer membrane proteins using mass spectrometry.PagP activation in the outer membrane triggers R3 core oligosaccharide truncation in the cytoplasm of Escherichia coli O157:H7.Detergent-mediated protein aggregation.PhoPQ regulates acidic glycerophospholipid content of the Salmonella Typhimurium outer membrane.Mechanistic studies of the biogenesis and folding of outer membrane proteins in vitro and in vivo: what have we learned to date?UVliPiD: A UVPD-Based Hierarchical Approach for De Novo Characterization of Lipid A Structures.Energetics of side-chain partitioning of β-signal residues in unassisted folding of a transmembrane β-barrel protein.Double tryptophan exciton probe to gauge proximal side chains in proteins: augmentation at low temperature.Malleability of the folding mechanism of the outer membrane protein PagP: parallel pathways and the effect of membrane elasticity.Characterizing the assembly of the Sup35 yeast prion fragment, GNNQQNY: structural changes accompany a fiber-to-crystal switch.Perturbations of Native Membrane Protein Structure in Alkyl Phosphocholine Detergents: A Critical Assessment of NMR and Biophysical Studies.Approaches for Preparation and Biophysical Characterization of Transmembrane β-BarrelsThermodynamic, structural and functional properties of membrane protein inclusion bodies are analogous to purified counterparts: case study from bacteria and humans
P2860
Q27664381-6BAFED21-CB94-46A7-A115-1AE0B145A722Q28828313-450A2008-1CB2-46F9-A158-C449E09A9726Q28828316-B87DCD63-F713-4034-B37B-DC9A377A355BQ30152682-93D65A41-26A2-43D3-BCBC-D6F99EE38E9AQ30152889-87339205-BD9A-41CD-ADDB-32608F00739BQ30153272-41BFF988-F54B-4D61-B9A2-3B859A8C2901Q30153476-BB219E9C-CC7B-4D35-80C0-1BFF15AA85ECQ30155073-7206D5E4-B680-4ABB-A7A7-886AD1D10D1DQ30155201-9AA83227-D47F-4BEE-BF68-BE79D920B262Q30155509-0855914E-91CB-420F-B37D-47D74EE7313AQ30157115-57EDD144-DE28-42E9-93CC-FE21299C7BBEQ30157760-223B4BAE-1C4C-4C52-9A8E-286110A7D3DBQ30157764-A5DC346D-8285-406F-B1CD-3D6B1B40AB78Q30357679-303FAEE3-A704-4297-BB12-AF37E9EFFF41Q30388800-98D9447D-7C75-480C-9A8E-C94EBB8634B2Q36392088-308F4B3F-D7B8-4493-85A6-0C5FD57130A0Q36450409-6EE25543-0D79-4FE3-85B8-9C85A298973FQ37222618-03922A85-2ABD-4AD2-8FC9-A77F641FDE8BQ37222622-13F1494F-DAD0-4A1B-A82D-BE92EA2033EBQ37571452-5D5050F7-90BB-44A9-A83E-8B67BC92C016Q38194733-F47578C6-5E43-4FBB-B3E4-983CE363A584Q40803203-626E2056-4CB4-4A2C-8A40-B3B4EE09A4D8Q41073405-D69E5CDC-9686-4417-BD5F-FFF8AE438836Q41171121-679EF86B-C03B-43D2-B2B2-95FC68263698Q41910574-9503A2E6-2F8F-45A9-A60A-5F8908DE690BQ42934740-99591ED6-98BE-4E3B-9A41-04230AF5C053Q54966402-E16ECFC4-2A5B-4D09-ADF3-26840B266B11Q57810611-C90EA36B-616D-431A-BD11-A1DFB2AB9809Q57810644-078D8058-2E08-4645-BF14-DF2D72A5B787
P2860
Gauging a hydrocarbon ruler by an intrinsic exciton probe.
description
2007 nî lūn-bûn
@nan
2007 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի մարտին հրատարակված գիտական հոդված
@hy
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
name
Gauging a hydrocarbon ruler by an intrinsic exciton probe.
@ast
Gauging a hydrocarbon ruler by an intrinsic exciton probe.
@en
type
label
Gauging a hydrocarbon ruler by an intrinsic exciton probe.
@ast
Gauging a hydrocarbon ruler by an intrinsic exciton probe.
@en
prefLabel
Gauging a hydrocarbon ruler by an intrinsic exciton probe.
@ast
Gauging a hydrocarbon ruler by an intrinsic exciton probe.
@en
P2093
P2860
P356
P1433
P1476
Gauging a hydrocarbon ruler by an intrinsic exciton probe
@en
P2093
Catherine Michaux
Chris Neale
M Adil Khan
Robert W Woody
Russell E Bishop
Régis Pomès
P2860
P304
P356
10.1021/BI602526K
P407
P577
2007-03-22T00:00:00Z