Validation of the single-stranded channel conformation of gramicidin A by solid-state NMR.
about
The magic of bicelles lights up membrane protein structureAntimicrobial peptides in 2014Insights into the Mechanism of Action of Bactericidal LipophosphonoxinspH-Dependent lytic peptides discovered by phage display.Orientation determination of interfacial beta-sheet structures in situModulation of concentration fluctuations in phase-separated lipid membranes by polypeptide insertionSpin-labeled gramicidin a: channel formation and dissociation.Activities of temporin family peptides against the chytrid fungus (Batrachochytrium dendrobatidis) associated with global amphibian declines.A "Holey" supramolecular approach to the detection of enzyme activity.Gramicidin-perforated patch recording revealed the oscillatory nature of secretory Cl- movements in salivary acinar cellsRational design, synthesis, and biological evaluation of lactam-bridged gramicidin A analogues: discovery of a low-hemolytic antibacterial peptide.Proton mobilities in water and in different stereoisomers of covalently linked gramicidin A channels.Monitoring gramicidin conformations in membranes: a fluorescence approach.A synthetic S6 segment derived from KvAP channel self-assembles, permeabilizes lipid vesicles, and exhibits ion channel activity in bilayer lipid membrane.Interfacial positioning and stability of transmembrane peptides in lipid bilayers studied by combining hydrogen/deuterium exchange and mass spectrometry.A helix-loop-helix peptide at the upper lip of the active site cleft of lysozyme confers potent antimicrobial activity with membrane permeabilization action.Resolution enhancement in solid-state NMR of oriented membrane proteins by anisotropic differential linebroadening.Simultaneous encapsulation of an infinite T4(0)A(0)6(0) water tape and discrete water hexamers in a hydrogen-bonded Ag(I) supramolecular framework.Antibacterial activities of temporin A analogs.Tapes of Cyclic Water Tetramers in the Double-Helical Complex[Cd2(bpa)2Cl4]·6 H2O
P2860
Q26991483-6BAF9C28-6818-4EA4-B68D-ADBDB24DBCCCQ27027316-2F7911D8-1B80-4A18-A1DE-F0BAF3D01D8FQ28551859-DFDCFF4F-DB81-47CF-8C56-6D806A9AE660Q33243402-7999E401-02A4-473E-BB3D-952449418D44Q33958543-C47A98EE-5BDE-4203-9292-568B73EB4BE2Q34178320-BE0F24CB-A721-4CF8-8B56-E9F91A22AD62Q34187789-F404FB13-0550-4870-A5B6-52B869A2366FQ34734459-5D8894D3-5798-4BF8-B8F3-98877CD418D3Q35602382-E1DDD8BB-87C0-4D36-85AD-95CD6E8ABBACQ36436709-8A947E27-BE1D-4B82-B949-36B391D4ABB4Q38928471-331C2B52-39C4-48C6-86AB-E233CA15EB58Q40161359-6125A716-E53D-4F8B-BD1C-7AC26C75C9F1Q40293238-B1800BF5-EAB1-4DBB-A533-EEE73D331357Q42813550-4652CBA7-076D-4E63-B1D3-3A8B5D0963D2Q43660537-4A041291-0161-4B54-BC27-5D34615967ADQ43740251-24340007-724B-4725-AA97-4C5A9F4E6A12Q49859235-0451CFD2-C95B-4908-8209-7A006C5BB29CQ53564048-B5A15A42-D943-44CC-9456-EBC12DC186B3Q54040820-3046DFC5-D90F-47E9-B5F3-56E76AD726C3Q57732947-1B210FD5-F13D-4051-B671-AD23EDBCC13F
P2860
Validation of the single-stranded channel conformation of gramicidin A by solid-state NMR.
description
1999 nî lūn-bûn
@nan
1999年の論文
@ja
1999年学术文章
@wuu
1999年学术文章
@zh-cn
1999年学术文章
@zh-hans
1999年学术文章
@zh-my
1999年学术文章
@zh-sg
1999年學術文章
@yue
1999年學術文章
@zh
1999年學術文章
@zh-hant
name
Validation of the single-stran ...... amicidin A by solid-state NMR.
@ast
Validation of the single-stran ...... amicidin A by solid-state NMR.
@en
type
label
Validation of the single-stran ...... amicidin A by solid-state NMR.
@ast
Validation of the single-stran ...... amicidin A by solid-state NMR.
@en
prefLabel
Validation of the single-stran ...... amicidin A by solid-state NMR.
@ast
Validation of the single-stran ...... amicidin A by solid-state NMR.
@en
P2093
P2860
P356
P1476
Validation of the single-stran ...... amicidin A by solid-state NMR.
@en
P2093
P2860
P304
P356
10.1073/PNAS.96.14.7910
P407
P577
1999-07-01T00:00:00Z