Structure and orientation of antibiotic peptide alamethicin in phospholipid bilayers as revealed by chemical shift oscillation analysis of solid state nuclear magnetic resonance and molecular dynamics simulation.
about
Length-Dependent Formation of Transmembrane Pores by 310-Helical α-Aminoisobutyric Acid Foldamers.Simulations of Membrane-Disrupting Peptides I: Alamethicin Pore Stability and Spontaneous InsertionSarconesin: Blowfly Larval Excretions and Secretions With Antibacterial PropertiesStructure Determination of Membrane Peptides and Proteins by Solid-State NMR
P2860
Structure and orientation of antibiotic peptide alamethicin in phospholipid bilayers as revealed by chemical shift oscillation analysis of solid state nuclear magnetic resonance and molecular dynamics simulation.
description
2015 nî lūn-bûn
@nan
2015年の論文
@ja
2015年論文
@yue
2015年論文
@zh-hant
2015年論文
@zh-hk
2015年論文
@zh-mo
2015年論文
@zh-tw
2015年论文
@wuu
2015年论文
@zh
2015年论文
@zh-cn
name
Structure and orientation of a ...... molecular dynamics simulation.
@en
type
label
Structure and orientation of a ...... molecular dynamics simulation.
@en
prefLabel
Structure and orientation of a ...... molecular dynamics simulation.
@en
P2093
P1476
Structure and orientation of a ...... molecular dynamics simulation.
@en
P2093
Daisuke Ishioka
Daisuke Mishima
Kazushi Norisada
Kazuyoshi Ueda
Kiyonobu Yokota
Namsrai Javkhlantugs
Takashi Nagao
P304
P356
10.1016/J.BBAMEM.2015.07.019
P433
P577
2015-08-03T00:00:00Z