Use of a single glycine residue to determine the tilt and orientation of a transmembrane helix. A new structural label for infrared spectroscopy
about
C-deuterated alanine: a new label to study membrane protein structure using site-specific infrared dichroism.The transmembrane homotrimer of ADAM 1 in model lipid bilayers.Geometry and intrinsic tilt of a tryptophan-anchored transmembrane alpha-helix determined by (2)H NMRProton conduction through the M2 protein of the influenza A virus; a quantitative, mechanistic analysis of experimental data.Sequence determinants of the energetics of folding of a transmembrane four-helix-bundle protein.How do helix-helix interactions help determine the folds of membrane proteins? Perspectives from the study of homo-oligomeric helical bundles.Roles of the histidine and tryptophan side chains in the M2 proton channel from influenza A virus.The chemical and dynamical influence of the anti-viral drug amantadine on the M2 proton channel transmembrane domain.Environment Polarity in Proteins Mapped Noninvasively by FTIR SpectroscopyProton transport behavior through the influenza A M2 channel: insights from molecular simulation.Site-specific dichroism analysis utilizing transmission FTIR.Two different conformations in hepatitis C virus p7 protein account for proton transport and dye release.Gating mechanism of the influenza A M2 channel revealed by 1D and 2D IR spectroscopies.The conformation of the pore region of the M2 proton channel depends on lipid bilayer environment.Determination of membrane protein stability via thermodynamic coupling of folding to thiol-disulfide interchange.Disorder influence on linear dichroism analyses of smectic phases.Carbon-deuterium vibrational probes of peptide conformation: alanine dipeptide and glycine dipeptide.
P2860
Q30329471-96BBD5ED-AF75-4020-9B42-B03327B65AC0Q30443798-07DDADA0-FD8E-41F7-8BD0-5BEDD32CB9CDQ30717237-C21C583C-B59A-49E4-88F9-876F272A7E04Q30825019-7889216E-F7DC-4A6F-8F25-7787457661FFQ34064987-D9E5BFAA-238E-41EC-BCD3-DB234741597DQ35089609-1B12D389-B75B-4CAA-9868-2A44493536D2Q35217953-3791B78E-31B9-4B03-8BB9-57F4DA02F339Q35881242-9B1BBBA2-36E5-4F82-9A20-86BBF49D8F97Q35926279-1FD1F018-A6C8-4999-B27C-64EC8DEEEC36Q36129061-98E20344-446E-4619-AAAA-103C4BA4D00AQ40256414-2353E573-4372-4A87-9F17-41C8417BA92CQ41856223-DE20945E-265B-4752-88D5-11ED04870888Q42021816-9E3737C9-9F05-425E-8D4E-90E6466672F7Q42083512-B2841CD3-CB3A-489F-A3D0-B00E3327608FQ42109644-8AB366F0-87C5-4616-8B22-CB11FB0C657AQ43203020-BC04982A-7A49-462B-8B98-7557C0336CABQ46067348-D89BF249-DFE9-4543-B3E6-B476CACC5945
P2860
Use of a single glycine residue to determine the tilt and orientation of a transmembrane helix. A new structural label for infrared spectroscopy
description
2000 nî lūn-bûn
@nan
2000 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2000年の論文
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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 single glycine residu ...... abel for infrared spectroscopy
@ast
Use of a single glycine residu ...... abel for infrared spectroscopy
@en
type
label
Use of a single glycine residu ...... abel for infrared spectroscopy
@ast
Use of a single glycine residu ...... abel for infrared spectroscopy
@en
prefLabel
Use of a single glycine residu ...... abel for infrared spectroscopy
@ast
Use of a single glycine residu ...... abel for infrared spectroscopy
@en
P2093
P2860
P1433
P1476
Use of a single glycine residu ...... abel for infrared spectroscopy
@en
P2093
P2860
P304
P356
10.1016/S0006-3495(00)76547-7
P407
P577
2000-12-01T00:00:00Z