Solid-state NMR studies of the structure, dynamics, and assembly of beta-sheet membrane peptides and alpha-helical membrane proteins with antibiotic activities.
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Structural basis for the function and inhibition of an influenza virus proton channelStructure and Membrane Interactions of the Antibiotic Peptide Dermadistinctin K by Multidimensional Solution and Oriented 15N and 31P Solid-State NMR SpectroscopyAntimicrobial peptide protegrin-3 adopt an antiparallel dimer in the presence of DPC micelles: a high-resolution NMR studyStructure and mechanism of beta-hairpin antimicrobial peptides in lipid bilayers from solid-state NMR spectroscopy.Paramagnetic Cu(II) for probing membrane protein structure and function: inhibition mechanism of the influenza M2 proton channel.Structural basis for proton conduction and inhibition by the influenza M2 protein.Conformational changes of an ion channel detected through water-protein interactions using solid-state NMR spectroscopy.Structure and dynamics of cationic membrane peptides and proteins: insights from solid-state NMR.Computational studies of colicin insertion into membranes: the closed statePractical use of chemical shift databases for protein solid-state NMR: 2D chemical shift maps and amino-acid assignment with secondary-structure informationStructures of β-hairpin antimicrobial protegrin peptides in lipopolysaccharide membranes: mechanism of gram selectivity obtained from solid-state nuclear magnetic resonance.Solid-state NMR spectroscopy on complex biomolecules.Molecular understanding of a potential functional link between antimicrobial and amyloid peptides.Lipid-dependent pore formation by antimicrobial peptides arenicin-2 and melittin demonstrated by their proton transfer activity.Immobilization of the influenza A M2 transmembrane peptide in virus envelope-mimetic lipid membranes: a solid-state NMR investigation.Aromatic spectral editing techniques for magic-angle-spinning solid-state NMR spectroscopy of uniformly (13)C-labeled proteins.SedNMR: a web tool for optimizing sedimentation of macromolecular solutes for SSNMR.
P2860
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P2860
Solid-state NMR studies of the structure, dynamics, and assembly of beta-sheet membrane peptides and alpha-helical membrane proteins with antibiotic activities.
description
2006 nî lūn-bûn
@nan
2006年の論文
@ja
2006年学术文章
@wuu
2006年学术文章
@zh-cn
2006年学术文章
@zh-hans
2006年学术文章
@zh-my
2006年学术文章
@zh-sg
2006年學術文章
@yue
2006年學術文章
@zh
2006年學術文章
@zh-hant
name
Solid-state NMR studies of the ...... ns with antibiotic activities.
@ast
Solid-state NMR studies of the ...... ns with antibiotic activities.
@en
type
label
Solid-state NMR studies of the ...... ns with antibiotic activities.
@ast
Solid-state NMR studies of the ...... ns with antibiotic activities.
@en
prefLabel
Solid-state NMR studies of the ...... ns with antibiotic activities.
@ast
Solid-state NMR studies of the ...... ns with antibiotic activities.
@en
P356
P1476
Solid-state NMR studies of the ...... ns with antibiotic activities.
@en
P2093
P304
P356
10.1021/AR040037E
P407
P577
2006-03-01T00:00:00Z