Use of a new label, (13)==(18)O, in the determination of a structural model of phospholamban in a lipid bilayer. Spatial restraints resolve the ambiguity arising from interpretations of mutagenesis data.
about
A new method to model membrane protein structure based on silent amino acid substitutions.C-deuterated alanine: a new label to study membrane protein structure using site-specific infrared dichroism.Strength of a bifurcated H bond.Assessment of amide I spectroscopic maps for a gas-phase peptide using IR-UV double-resonance spectroscopy and density functional theory calculationsThe transmembrane homotrimer of ADAM 1 in model lipid bilayers.Residue-specific structural kinetics of proteins through the union of isotope labeling, mid-IR pulse shaping, and coherent 2D IR spectroscopy.Data-driven docking for the study of biomolecular complexes.Model of a putative pore: the pentameric alpha-helical bundle of SARS coronavirus E protein in lipid bilayers.Mapping the energy surface of transmembrane helix-helix interactionsEvaluation of the ordering of membranes in multilayer stacks built on an ATR-FTIR germanium crystal with atomic force microscopy: the case of the H(+),K(+)-ATPase-containing gastric tubulovesicle membranes.Design, synthesis, and photochemical validation of peptide linchpins containing the S,S-tetrazine phototriggerTidal surge in the M2 proton channel, sensed by 2D IR spectroscopy.How do helix-helix interactions help determine the folds of membrane proteins? Perspectives from the study of homo-oligomeric helical bundles.Environment Polarity in Proteins Mapped Noninvasively by FTIR SpectroscopyThermally induced protein unfolding probed by isotope-edited IR spectroscopy.A bifunctional spin label reports the structural topology of phospholamban in magnetically-aligned bicelles.Structure and ion channel activity of the human respiratory syncytial virus (hRSV) small hydrophobic protein transmembrane domain.Empirical amide I vibrational frequency map: application to 2D-IR line shapes for isotope-edited membrane peptide bundles.The strong dimerization of the transmembrane domain of the fibroblast growth factor receptor (FGFR) is modulated by C-terminal juxtamembrane residues.2D IR cross peaks reveal hydrogen-deuterium exchange with single residue specificity.Structural constraints on the transmembrane and juxtamembrane regions of the phospholamban pentamer in membrane bilayers: Gln29 and Leu52.2DIR spectroscopy of human amylin fibrils reflects stable β-sheet structure.Contribution of energy values to the analysis of global searching molecular dynamics simulations of transmembrane helical bundles.Site-specific dichroism analysis utilizing transmission FTIR.Modeling sample disorder in site-specific dichroism studies of uniaxial systems.Probing the helical tilt and dynamic properties of membrane-bound phospholamban in magnetically aligned bicelles using electron paramagnetic resonance spectroscopy.Development and validation of transferable amide I vibrational frequency maps for peptides.Two different conformations in hepatitis C virus p7 protein account for proton transport and dye release.The design and synthesis of alanine-rich α-helical peptides constrained by an S,S-tetrazine photochemical trigger: a fragment union approachGating mechanism of the influenza A M2 channel revealed by 1D and 2D IR spectroscopies.Theoretical Sum Frequency Generation Spectroscopy of Peptides.Conductance and amantadine binding of a pore formed by a lysine-flanked transmembrane domain of SARS coronavirus envelope protein.Computational design of a water-soluble analog of phospholamban.Transmembrane helices that form two opposite homodimeric interactions: an asparagine scan study of alphaM and beta2 integrins.Disorder influence on linear dichroism analyses of smectic phases.Modeling the structure of the respiratory syncytial virus small hydrophobic protein by silent-mutation analysis of global searching molecular dynamics.Sarcolipin, the shorter homologue of phospholamban, forms oligomeric structures in detergent micelles and in liposomes.Topology of the Salmonella invasion protein SipB in a model bilayer.Modeling membrane proteins utilizing information from silent amino acid substitutions.Phospholemman transmembrane structure reveals potential interactions with Na+/K+-ATPase.
P2860
Q30328399-029579C1-B0A7-45D8-B21A-A722AEFE846EQ30329471-4CC188DF-6C21-4FFF-A712-B523C847A773Q30359748-4E84B673-0C3B-425A-952D-3C70D2DAA25AQ30363602-82522D0B-6745-4E10-92F8-AC8EE4FA2824Q30443798-1F790B8B-4FBF-4211-BEF6-06564ABE1329Q30474383-70209DDF-7696-48CD-A4F4-85B3F90DF8CAQ30980755-66AEDB6D-3B9F-40C6-AA0F-6B700A786114Q33995815-1C789A80-7CE2-4023-A0E3-FBFBC528DF9CQ34176789-A85631C9-6589-465A-B04B-03488787F4A8Q34186670-3D5574CF-00E6-4885-BAD2-01BC9DDC6F59Q34316686-FF728A3C-E576-42BE-8782-3E69DF02399AQ34794456-054F8BFB-313A-4E3B-BB10-C2282164D8D9Q35089609-7BC6189C-53CF-483D-BB81-279415D5FCBDQ35926279-9B79BB7C-A8F9-4DA6-8DEC-0FF83C77116CQ36294499-684A266C-3472-4F89-B2FD-8D5B73EE7DA9Q36474003-3E3BEA9C-6FC6-4AD1-A080-F072ABFF16B0Q36575529-9EE2F6F2-C91C-4E11-9804-831D79E1C4EAQ37077870-2E36CD14-6F22-4D80-95B2-96695C72DA62Q37255433-1557F709-43ED-4F16-B0A1-81E203ED3ED3Q37265693-BD013959-954E-4878-92D3-53DC5E274AD7Q37275638-B89E9990-3CF7-491E-9F7B-EF7240A4CF85Q38751982-9FE0C9A6-6655-4B29-8606-FDFDA4320045Q40208140-2D447EC0-7D8A-4A4B-B32B-192E31BE5B9EQ40256414-2F5AAC81-B2CC-4BE5-8DF1-F1C376202452Q40278722-CF32A67C-0938-45FF-9B9F-7E6AF40D448DQ40891582-DAEDC1D3-FF01-4538-BC3B-B08776481169Q40935469-C0B82829-44DF-449F-811A-AB3009A09269Q41856223-6C571AA8-C0DC-4780-8E56-DBD131BD8E96Q41927375-4DC7512B-60B8-4772-814E-7BBCD62B9864Q42021816-421B0DF7-C4EE-4A3E-A2AA-99C453DB33D4Q42071354-6F9C6E7E-E55A-4CF1-A3FD-1008DF6B531CQ42111936-12DF94BC-F15D-4D97-A703-A2A659AE4409Q43137315-2683FC02-FE19-4FDC-972B-3248321BBAEDQ43157337-6C993131-10DE-4E77-9B7C-5C0BCCED5837Q43203020-05CCD738-BD89-4129-B0A5-FBF2E8721976Q43205497-77E11BD7-2599-4C41-A600-D381402FD366Q43645352-BE33CAD7-B6ED-4B07-A3AA-C1068B3A7169Q48558570-817CDFF2-983F-4FEC-BE64-EC2787D69906Q51888002-243098A9-15B9-4004-AE14-4581D71BA019Q53848398-08E16028-1B99-4C90-8F54-502F16067E6B
P2860
Use of a new label, (13)==(18)O, in the determination of a structural model of phospholamban in a lipid bilayer. Spatial restraints resolve the ambiguity arising from interpretations of mutagenesis data.
description
2000 nî lūn-bûn
@nan
2000 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Use of a new label, (13)==(18) ...... retations of mutagenesis data.
@ast
Use of a new label, (13)==(18) ...... retations of mutagenesis data.
@en
type
label
Use of a new label, (13)==(18) ...... retations of mutagenesis data.
@ast
Use of a new label, (13)==(18) ...... retations of mutagenesis data.
@en
prefLabel
Use of a new label, (13)==(18) ...... retations of mutagenesis data.
@ast
Use of a new label, (13)==(18) ...... retations of mutagenesis data.
@en
P356
P1476
Use of a new label, (13)==(18) ...... pretations of mutagenesis data
@en
P2093
P304
P356
10.1006/JMBI.2000.3885
P407
P577
2000-07-01T00:00:00Z