Ferdani, Riccardo <br/><br/>
Glycine position permutations and peptide length alterations change the aggregation state and efficacy of ion-conducting, pore-forming amphiphiles.  [electronic resource] 

 -  Chemical communications (Cambridge, England)  Jan 2006 
 - 439-41 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, N.I.H., Extramural 
<br/><br/><label>ISSN: </label>1359-7345 
<br/><br/><label>Standard No.: </label>10.1039/b514806p  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Biological Transport<br/>Dihydroxyphenylalanine--chemistry<br/>Fluoresceins--chemistry<br/>Glycine--chemistry<br/>Ions<br/>Lipid Bilayers--chemistry<br/>Liposomes--chemistry<br/>Oligopeptides--chemistry<br/>Phosphatidylcholines--chemistry<br/>Porosity<br/>Surface-Active Agents--chemistry<br/>Time Factors