AbstractWe have investigated the x-ray scattering signal of highly aligned multilayers of the zwitterionic lipid 1,2-dimyristoyl-sn-glycero-3-phosphatidylcholine containing pores formed by the antimicrobial peptide alamethicin as a function of the peptide/lipid ratio. We are able to obtain information on the structure factor of the pore fluid, which then yields the interaction potential between pores in the plane of the bilayers. Aside from a hard core with a radius corresponding to the geometric radius of the pore, we find a repulsive lipid-mediated interaction with a range of ∼30Å and a contact value of 2.4 kBT. This result is in qualitative agreement with recent theoretical models
A detailed knowledge of the interaction between bacterial membranes and antibiotics provides importa...
A detailed knowledge of the interaction between bacterial membranes and antibiotics provides importa...
X-ray scattering features induced by aggregates of alamethicin (Alm) were obtained in oriented stack...
ABSTRACT Wehave investigated the x-ray scattering signal of highly alignedmultilayers of the zwitter...
We have investigated the X-ray scattering signal of highly aligned multilayers of the zwitterionic l...
AbstractWe have investigated the x-ray scattering signal of highly aligned multilayers of the zwitte...
AbstractWe investigated the X-ray scattering signal of highly aligned multilayers of the zwitterioni...
AbstractWe investigated the X-ray scattering signal of highly aligned multilayers of the zwitterioni...
Alamethicin is a well-studied channel-forming peptide that has a prototypical amphipathic helix stru...
AbstractWe reconstructed the electron density profile of the alamethicin-induced transmembrane pore ...
Alamethicin is a transmembrane ion channel at low concentration, and a lytic agent of cell membrane ...
Cell membranes are complex mixtures of lipids, proteins, and other molecules that serve as active, s...
A detailed knowledge of the interaction between bacterial membranes and antibiotics provides importa...
A detailed knowledge of the interaction between bacterial membranes and antibiotics provides importa...
A detailed knowledge of the interaction between bacterial membranes and antibiotics provides importa...
A detailed knowledge of the interaction between bacterial membranes and antibiotics provides importa...
A detailed knowledge of the interaction between bacterial membranes and antibiotics provides importa...
X-ray scattering features induced by aggregates of alamethicin (Alm) were obtained in oriented stack...
ABSTRACT Wehave investigated the x-ray scattering signal of highly alignedmultilayers of the zwitter...
We have investigated the X-ray scattering signal of highly aligned multilayers of the zwitterionic l...
AbstractWe have investigated the x-ray scattering signal of highly aligned multilayers of the zwitte...
AbstractWe investigated the X-ray scattering signal of highly aligned multilayers of the zwitterioni...
AbstractWe investigated the X-ray scattering signal of highly aligned multilayers of the zwitterioni...
Alamethicin is a well-studied channel-forming peptide that has a prototypical amphipathic helix stru...
AbstractWe reconstructed the electron density profile of the alamethicin-induced transmembrane pore ...
Alamethicin is a transmembrane ion channel at low concentration, and a lytic agent of cell membrane ...
Cell membranes are complex mixtures of lipids, proteins, and other molecules that serve as active, s...
A detailed knowledge of the interaction between bacterial membranes and antibiotics provides importa...
A detailed knowledge of the interaction between bacterial membranes and antibiotics provides importa...
A detailed knowledge of the interaction between bacterial membranes and antibiotics provides importa...
A detailed knowledge of the interaction between bacterial membranes and antibiotics provides importa...
A detailed knowledge of the interaction between bacterial membranes and antibiotics provides importa...
X-ray scattering features induced by aggregates of alamethicin (Alm) were obtained in oriented stack...