Orientation of the Escherichia coli outer membrane protein OmpX in phospholipid bilayer membranes determined by solid-State NMR.
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Structure determination of membrane proteins by nuclear magnetic resonance spectroscopyThe magic of bicelles lights up membrane protein structureHigh-resolution membrane protein structure by joint calculations with solid-state NMR and X-ray experimental dataStructure of the Na,K-ATPase regulatory protein FXYD2b in micelles: Implications for membrane–water interfacial argininesMembrane proteins in their native habitat as seen by solid-state NMR spectroscopyMethionine mutations of outer membrane protein X influence structural stability and beta-barrel unfoldingDifferential contribution of tryptophans to the folding and stability of the attachment invasion locus transmembrane β-barrel from Yersinia pestis.Membrane protein structure determination in membrana.Modulating lipid dynamics and membrane fluidity to drive rapid folding of a transmembrane barrel.AssignFit: a program for simultaneous assignment and structure refinement from solid-state NMR spectra.NMR structures of polytopic integral membrane proteins.Membrane protein structure determination: back to the membrane.A refinement protocol to determine structure, topology, and depth of insertion of membrane proteins using hybrid solution and solid-state NMR restraints.High quality NMR structures: a new force field with implicit water and membrane solvation for Xplor-NIH.Membrane protein structure and dynamics from NMR spectroscopy.Solid state NMR strategy for characterizing native membrane protein structuresHigh resolution solid-state NMR spectroscopy of the Yersinia pestis outer membrane protein Ail in lipid membranes.On the combined analysis of ²H and ¹⁵N/¹H solid-state NMR data for determination of transmembrane peptide orientation and dynamicsA Practical Implicit Membrane Potential for NMR Structure Calculations of Membrane Proteins.When detergent meets bilayer: birth and coming of age of lipid bicelles.Bicelles: A natural 'molecular goniometer' for structural, dynamical and topological studies of molecules in membranes.Structure determination of membrane proteins in five easy piecesSecondary structure, backbone dynamics, and structural topology of phospholamban and its phosphorylated and Arg9Cys-mutated forms in phospholipid bilayers utilizing 13C and 15N solid-state NMR spectroscopy.Spectral editing at ultra-fast magic-angle-spinning in solid-state NMR: facilitating protein sequential signal assignment by HIGHLIGHT approach.Correlating lipid bilayer fluidity with sensitivity and resolution of polytopic membrane protein spectra by solid-state NMR spectroscopy.Expression, refolding, and initial structural characterization of the Y. pestis Ail outer membrane protein in lipids.Recent Advances in the Application of Solution NMR Spectroscopy to Multi-Span Integral Membrane Proteins.Probing the interaction of Arg9Cys mutated phospholamban with phospholipid bilayers by solid-state NMR spectroscopy.
P2860
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P2860
Orientation of the Escherichia coli outer membrane protein OmpX in phospholipid bilayer membranes determined by solid-State NMR.
description
2008 nî lūn-bûn
@nan
2008 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
Orientation of the Escherichia ...... determined by solid-State NMR.
@ast
Orientation of the Escherichia ...... determined by solid-State NMR.
@en
type
label
Orientation of the Escherichia ...... determined by solid-State NMR.
@ast
Orientation of the Escherichia ...... determined by solid-State NMR.
@en
prefLabel
Orientation of the Escherichia ...... determined by solid-State NMR.
@ast
Orientation of the Escherichia ...... determined by solid-State NMR.
@en
P2860
P356
P1433
P1476
Orientation of the Escherichia ...... determined by solid-State NMR.
@en
P2093
Francesca M Marassi
P2860
P304
P356
10.1021/BI800362B
P407
P577
2008-06-01T00:00:00Z