Conformation of peptides in lipid membranes studied by x-ray grazing incidence scattering.
about
Interactions of alamethicin with model cell membranes investigated using sum frequency generation vibrational spectroscopy in real time in situObserving a model ion channel gating action in model cell membranes in real time in situ: membrane potential change induced alamethicin orientation change.Peptide antimicrobial agents.Interactions of membrane-active peptides with thick, neutral, nonzwitterionic bilayers.Integration of ganglioside GT1b receptor into DPPE and DPPC phospholipid monolayers: an X-ray reflectivity and grazing-incidence diffraction study.Alamethicin in lipid bilayers: combined use of X-ray scattering and MD simulations.Structure and alignment of the membrane-associated peptaibols ampullosporin A and alamethicin by oriented 15N and 31P solid-state NMR spectroscopy.The roles of antimicrobial peptides in innate host defense.In situ molecular level studies on membrane related peptides and proteins in real time using sum frequency generation vibrational spectroscopy.Antimicrobial peptides and induced membrane curvature: geometry, coordination chemistry, and molecular engineering.Membrane-active peptides from marine organisms--antimicrobials, cell-penetrating peptides and peptide toxins: applications and prospects.Conformation, self-aggregation, and membrane interaction of peptaibols as studied by pulsed electron double resonance spectroscopy.Structure of magainin and alamethicin in model membranes studied by x-ray reflectivityInsertion of lipidated Ras proteins into lipid monolayers studied by infrared reflection absorption spectroscopy (IRRAS).A thermodynamic approach to alamethicin pore formationIn situ muGISAXS: II. Thaumatin crystal growth kineticStructure of self-aggregated alamethicin in ePC membranes detected by pulsed electron-electron double resonance and electron spin echo envelope modulation spectroscopiesPeptide model helices in lipid membranes: insertion, positioning, and lipid response on aggregation studied by X-ray scattering.Lipid-packing perturbation of model membranes by pH-responsive antimicrobial peptides.What can machine learning do for antimicrobial peptides, and what can antimicrobial peptides do for machine learning?Hierarchical, self-similar structure in native squid pen.
P2860
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P2860
Conformation of peptides in lipid membranes studied by x-ray grazing incidence scattering.
description
2004 nî lūn-bûn
@nan
2004年の論文
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2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
2004年论文
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2004年论文
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name
Conformation of peptides in li ...... grazing incidence scattering.
@en
type
label
Conformation of peptides in li ...... grazing incidence scattering.
@en
prefLabel
Conformation of peptides in li ...... grazing incidence scattering.
@en
P2860
P1433
P1476
Conformation of peptides in li ...... grazing incidence scattering.
@en
P2093
Alexander Spaar
Christian Münster
P2860
P304
P356
10.1529/BIOPHYSJ.104.040667
P407
P50
P577
2004-07-01T00:00:00Z