Conformation of alamethicin in oriented phospholipid bilayers determined by (15)N solid-state nuclear magnetic resonance.
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The role of hydrophobic interactions in positioning of peripheral proteins in membranesVolatile emission in bracken fern is induced by jasmonates but not by Spodoptera littoralis or Strongylogaster multifasciata herbivoryInduction of morphological changes in model lipid membranes and the mechanism of membrane disruption by a large scorpion-derived pore-forming peptide.Peptide aggregation and pore formation in a lipid bilayer: a combined coarse-grained and all atom molecular dynamics study.Alamethicin aggregation in lipid membranes.Interactions of alamethicin with model cell membranes investigated using sum frequency generation vibrational spectroscopy in real time in situAntimicrobial peptides in toroidal and cylindrical pores.Conformational changes in alamethicin associated with substitution of its alpha-methylalanines with leucines: a FTIR spectroscopic analysis and correlation with channel kineticsDetermination of the orientation and dynamics of ergosterol in model membranes using uniform 13C labeling and dynamically averaged 13C chemical shift anisotropies as experimental restraints.Mechanisms of peptide-induced pore formation in lipid bilayers investigated by oriented 31P solid-state NMR spectroscopy.Influence of the membrane dipole potential on peptide binding to lipid bilayers.Techniques and applications of NMR to membrane proteins.Observing a model ion channel gating action in model cell membranes in real time in situ: membrane potential change induced alamethicin orientation change.Dependence of Alamethicin Membrane Orientation on the Solution Concentration.Interactions of membrane-active peptides with thick, neutral, nonzwitterionic bilayers.Alamethicin in lipid bilayers: combined use of X-ray scattering and MD simulations.Lipid Fluid-Gel Phase Transition Induced Alamethicin Orientational Change Probed by Sum Frequency Generation Vibrational SpectroscopyStructure and alignment of the membrane-associated peptaibols ampullosporin A and alamethicin by oriented 15N and 31P solid-state NMR spectroscopy.In situ molecular level studies on membrane related peptides and proteins in real time using sum frequency generation vibrational spectroscopy.Insights into the mechanisms of action of host defence peptides from biophysical and structural investigations.The SMART model: Soft Membranes Adapt and Respond, also Transiently, in the presence of antimicrobial peptides.Structure of magainin and alamethicin in model membranes studied by x-ray reflectivitySize distribution of barrel-stave aggregates of membrane peptides: influence of the bilayer lateral pressure profile.Conformation of peptides in lipid membranes studied by x-ray grazing incidence scattering.Orientation and pore-forming mechanism of a scorpion pore-forming peptide bound to magnetically oriented lipid bilayers.Simulations of Membrane-Disrupting Peptides I: Alamethicin Pore Stability and Spontaneous InsertionA thermodynamic approach to alamethicin pore formationInteraction of alamethicin with ether-linked phospholipid bilayers: oriented circular dichroism, 31P solid-state NMR, and differential scanning calorimetry studies.Cholesterol reduces pardaxin's dynamics-a barrel-stave mechanism of membrane disruption investigated by solid-state NMR.Intramembrane water associated with TOAC spin-labeled alamethicin: electron spin-echo envelope modulation by D2O.Structure of self-aggregated alamethicin in ePC membranes detected by pulsed electron-electron double resonance and electron spin echo envelope modulation spectroscopiesInteraction of alamethicin pores in DMPC bilayers.The influence of different lipid environments on the structure and function of the hepatitis C virus p7 ion channel protein.Encapsulating Networks of Droplet Interface Bilayers in a Thermoreversible Organogel.Biophysical Investigations Elucidating the Mechanisms of Action of Antimicrobial Peptides and Their Synergism.On dating stages in prebiotic chemical evolutionStructure Determination of Membrane Peptides and Proteins by Solid-State NMR
P2860
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P2860
Conformation of alamethicin in oriented phospholipid bilayers determined by (15)N solid-state nuclear magnetic resonance.
description
2001 nî lūn-bûn
@nan
2001 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Conformation of alamethicin in ...... ate nuclear magnetic resonance
@nl
Conformation of alamethicin in ...... te nuclear magnetic resonance.
@ast
Conformation of alamethicin in ...... te nuclear magnetic resonance.
@en
type
label
Conformation of alamethicin in ...... ate nuclear magnetic resonance
@nl
Conformation of alamethicin in ...... te nuclear magnetic resonance.
@ast
Conformation of alamethicin in ...... te nuclear magnetic resonance.
@en
prefLabel
Conformation of alamethicin in ...... ate nuclear magnetic resonance
@nl
Conformation of alamethicin in ...... te nuclear magnetic resonance.
@ast
Conformation of alamethicin in ...... te nuclear magnetic resonance.
@en
P2093
P2860
P1433
P1476
Conformation of alamethicin in ...... te nuclear magnetic resonance.
@en
P2093
Adelhorst K
Bywater RP
Jakobsen HJ
Nielsen NC
Sørensen OW
Thomsen JK
P2860
P304
P356
10.1016/S0006-3495(01)75822-5
P407
P577
2001-09-01T00:00:00Z