Three-dimensional structure of (1-71)bacterioopsin solubilized in methanol/chloroform and SDS micelles determined by 15N-1H heteronuclear NMR spectroscopy
about
Quantification of helix-helix binding affinities in micelles and lipid bilayersThe hepatitis C virus RNA-dependent RNA polymerase membrane insertion sequence is a transmembrane segment.Transverse relaxation-optimized NMR spectroscopy with the outer membrane protein OmpX in dihexanoyl phosphatidylcholine micellesAssembly of a polytopic membrane protein structure from the solution structures of overlapping peptide fragments of bacteriorhodopsin.Structure of human immunodeficiency virus type 1 Vpr(34-51) peptide in micelle containing aqueous solutionStructure of a Double Transmembrane Fragment of a G-Protein-Coupled Receptor in MicellesFolding determinants of disulfide bond forming protein B explored by solution nuclear magnetic resonance spectroscopyIntrinsic Order and Disorder in the Bcl-2 Member Harakiri: Insights into Its Proapoptotic ActivityShifting hydrogen bonds may produce flexible transmembrane helices.NMR solution structure determination of membrane proteins reconstituted in detergent micelles.Strategies for dealing with conformational sampling in structural calculations of flexible or kinked transmembrane peptides.Invited review: GPCR structural characterization: Using fragments as building blocks to determine a complete structure.Escherichia coli diacylglycerol kinase: a case study in the application of solution NMR methods to an integral membrane protein.Electrospray ionization mass spectrometry as a tool to analyze hydrogen/deuterium exchange kinetics of transmembrane peptides in lipid bilayers.Techniques and applications of NMR to membrane proteins.NMR studies in dodecylphosphocholine of a fragment containing the seventh transmembrane helix of a G-protein-coupled receptor from Saccharomyces cerevisiae.An unfolding story of helical transmembrane proteins.Biophysical characterization of a recombinant aminopeptidase II from the thermophilic bacterium Bacillus stearothermophilus.Interaction of a two-transmembrane-helix peptide with lipid bilayers and dodecyl sulfate micelles.NMR Investigation of Structures of G-protein Coupled Receptor Folding Intermediates.Autonomous folding in the membrane proximal HIV peptide gp41(659-671): pH tuneability at micelle interfaces.Long-distance effects of site-directed mutations on backbone conformation in bacteriorhodopsin from solid state NMR of [1-13C]Val-labeled proteins.Effect of nanomolar concentrations of sodium dodecyl sulfate, a catalytic inductor of alpha-helices, on human calcitonin incorporation and channel formation in planar lipid membranes.Magic angle spinning NMR spectroscopy of membrane proteins.Direct observation of coherent oscillations in solution due to microheterogeneous environment.High resolution 1H nuclear magnetic resonance of a transmembrane peptide.A (13)C NMR study on [3-(13)C]-, [1-(13)C]Ala-, or [1-(13)C]Val-labeled transmembrane peptides of bacteriorhodopsin in lipid bilayers: insertion, rigid-body motions, and local conformational fluctuations at ambient temperature.Biosynthesis and purification of a hydrophobic peptide from transmembrane domains of G-protein-coupled CB2 receptor.Circular Dichroism of Proteins in Solution and at Interfaces
P2860
Q24645279-C41EA327-8CA6-472C-9E85-8DC632EE60ADQ27472921-C8F4C41C-1852-426D-8DAB-37CF70A347E0Q27630191-6FFF2411-7F57-4F90-B091-62B4FF10F9C2Q27633379-59D4DCDF-49EE-46D1-A58B-D6D827713BDFQ27639255-EE9C8D49-948E-437D-A3C4-190723D5ADDEQ27655003-5246F04A-88CC-43F9-8745-44C5B54A8F58Q27666760-302F6600-26EB-4AFB-86EC-4074D64AB9DCQ27670693-ADEA9A2B-950F-4019-9ADF-1309ECE61146Q27678953-B015EB13-813D-4783-91E9-CF76605D683AQ30164395-31B6580F-2DDC-4F83-865E-A2983959BE27Q30359168-F157D148-147F-45CE-8151-0DA215784E98Q30360845-1DE8B1D8-978D-4D15-B9AE-D22B2EA8D13CQ33915594-C3ADFCD0-79B3-481C-8863-2B6D844B1820Q35107673-AD18FA30-5682-4DFC-92C1-69CE889DB63EQ35809635-836DE33A-DE51-4B73-AE0E-FB0AA54A7820Q35850937-AE7CF776-E70A-4E9E-A43D-CAE3965CA30BQ36673002-7F9461CF-FFC1-4542-9AF2-6D1D67696410Q37582971-E0528D3F-553C-4E3E-81AE-8CBBB42D3261Q38687156-42FB8557-F15B-45FA-A65D-7A0212A3F1A5Q39173136-E4389D97-5B51-47FC-9159-EE6B0BA1D387Q39819718-BD67B079-AB07-42AA-BC8B-88135F1B05CAQ40146318-F26561F9-1D85-404C-8882-E71935239E50Q40291453-92BD0392-DA53-4F8E-BF4B-5C1BB222A1CCQ41395666-C983BBD8-796B-4EA7-AB10-DE09412EA176Q41883963-63196F85-09C5-407C-B3B2-533434824FE3Q42001858-F83F10DC-982A-41BE-B438-E5811E2D92C5Q43509610-1D371A68-083A-4E0A-87B9-2B46A18C452FQ46425016-1E3EE7C5-A4C8-4CAC-A547-6BCF1903FDE7Q57830260-2A4FC92C-54E5-46F6-ACC1-E2A42EB57BCA
P2860
Three-dimensional structure of (1-71)bacterioopsin solubilized in methanol/chloroform and SDS micelles determined by 15N-1H heteronuclear NMR spectroscopy
description
1994 nî lūn-bûn
@nan
1994 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1994 թվականի հունվարին հրատարակված գիտական հոդված
@hy
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
name
Three-dimensional structure of ...... heteronuclear NMR spectroscopy
@ast
Three-dimensional structure of ...... heteronuclear NMR spectroscopy
@en
Three-dimensional structure of ...... heteronuclear NMR spectroscopy
@nl
type
label
Three-dimensional structure of ...... heteronuclear NMR spectroscopy
@ast
Three-dimensional structure of ...... heteronuclear NMR spectroscopy
@en
Three-dimensional structure of ...... heteronuclear NMR spectroscopy
@nl
prefLabel
Three-dimensional structure of ...... heteronuclear NMR spectroscopy
@ast
Three-dimensional structure of ...... heteronuclear NMR spectroscopy
@en
Three-dimensional structure of ...... heteronuclear NMR spectroscopy
@nl
P2093
P2860
P1433
P1476
Three-dimensional structure of ...... heteronuclear NMR spectroscopy
@en
P2093
A S Arseniev
K V Pervushin
Musina LYu
Orekhov VYu
P2860
P304
P356
10.1111/J.1432-1033.1994.TB19973.X
P407
P577
1994-01-15T00:00:00Z