Proton affinity of the histidine-tryptophan cluster motif from the influenza A virus from ab initio molecular dynamics.
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Multiscale simulation reveals a multifaceted mechanism of proton permeation through the influenza A M2 proton channel.Hydrogen-bonded water molecules in the M2 channel of the influenza A virus guide the binding preferences of ammonium-based inhibitors.Activation and proton transport mechanism in influenza A M2 channelProton release from the histidine-tetrad in the M2 channel of the influenza A virus.M2 proton channel: toward a model of a primitive proton pump.Proton transfer in histidine-tryptophan heterodimers embedded in helium droplets.
P2860
Proton affinity of the histidine-tryptophan cluster motif from the influenza A virus from ab initio molecular dynamics.
description
2013 nî lūn-bûn
@nan
2013 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2013 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
name
Proton affinity of the histidi ...... ab initio molecular dynamics.
@ast
Proton affinity of the histidi ...... ab initio molecular dynamics.
@en
type
label
Proton affinity of the histidi ...... ab initio molecular dynamics.
@ast
Proton affinity of the histidi ...... ab initio molecular dynamics.
@en
prefLabel
Proton affinity of the histidi ...... ab initio molecular dynamics.
@ast
Proton affinity of the histidi ...... ab initio molecular dynamics.
@en
P2093
P2860
P1433
P1476
Proton affinity of the histidi ...... ab initio molecular dynamics.
@en
P2093
Arindam Bankura
Michael L Klein
Vincenzo Carnevale
P2860
P304
P356
10.1016/J.CHEMPHYS.2013.03.006
P577
2013-08-01T00:00:00Z