Free energy profile of the interaction between a monomer or a dimer of protegrin-1 in a specific binding orientation and a model lipid bilayer.
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Oligomerization of the antimicrobial peptide Protegrin-5 in a membrane-mimicking environment. Structural studies by high-resolution NMR spectroscopy.Implicit Membrane Investigation of the Stability of Antimicrobial Peptide β-Barrels and Arcs.Membrane interactions and pore formation by the antimicrobial peptide protegrin.Dimerization of protegrin-1 in different environments.Multiscale Models of Antibiotic Probiotics.Computational studies of protegrin antimicrobial peptides: a review.Thermodynamic analysis of protegrin-1 insertion and permeation through a lipid bilayerMultiscale models of the antimicrobial peptide protegrin-1 on gram-negative bacteria membranes.Computational studies of peptide-induced membrane pore formation.
P2860
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P2860
Free energy profile of the interaction between a monomer or a dimer of protegrin-1 in a specific binding orientation and a model lipid bilayer.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
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scientific article published on March 2010
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Free energy profile of the int ...... ion and a model lipid bilayer.
@en
Free energy profile of the int ...... ion and a model lipid bilayer.
@nl
type
label
Free energy profile of the int ...... ion and a model lipid bilayer.
@en
Free energy profile of the int ...... ion and a model lipid bilayer.
@nl
prefLabel
Free energy profile of the int ...... ion and a model lipid bilayer.
@en
Free energy profile of the int ...... ion and a model lipid bilayer.
@nl
P2860
P356
P1476
Free energy profile of the int ...... ion and a model lipid bilayer.
@en
P2093
Victor Vivcharuk
P2860
P304
P356
10.1021/JP909640G
P407
P577
2010-03-01T00:00:00Z