000 01430 a2200385 4500
005 20250515015241.0
264 0 _c20070426
008 200704s 0 0 eng d
022 _a1359-7345
024 7 _a10.1039/b514806p
_2doi
040 _aNLM
_beng
_cNLM
100 1 _aFerdani, Riccardo
245 0 0 _aGlycine position permutations and peptide length alterations change the aggregation state and efficacy of ion-conducting, pore-forming amphiphiles.
_h[electronic resource]
260 _bChemical communications (Cambridge, England)
_cJan 2006
300 _a439-41 p.
_bdigital
500 _aPublication Type: Journal Article; Research Support, N.I.H., Extramural
650 0 4 _aBiological Transport
650 0 4 _aDihydroxyphenylalanine
_xchemistry
650 0 4 _aFluoresceins
_xchemistry
650 0 4 _aGlycine
_xchemistry
650 0 4 _aIons
650 0 4 _aLipid Bilayers
_xchemistry
650 0 4 _aLiposomes
_xchemistry
650 0 4 _aOligopeptides
_xchemistry
650 0 4 _aPhosphatidylcholines
_xchemistry
650 0 4 _aPorosity
650 0 4 _aSurface-Active Agents
_xchemistry
650 0 4 _aTime Factors
700 1 _aPajewski, Robert
700 1 _aPajewska, Jolanta
700 1 _aSchlesinger, Paul H
700 1 _aGokel, George W
773 0 _tChemical communications (Cambridge, England)
_gno. 4
_gp. 439-41
856 4 0 _uhttps://doi.org/10.1039/b514806p
_zAvailable from publisher's website
999 _c16104985
_d16104985