Peptide secondary structure induced by a micellar phospholipidic interface: proton NMR conformational study of a lipopeptide

The conformational change of the model peptide Ac-K-G-R-G-D-G-amide induced by a phospholipidic interface was investigated by proton nuclear magnetic resonance (1H NMR). In aqueous solution, the free peptide is highly flexible and disordered, even in the presence of deuterated dodecyl-phosphocholine...

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Veröffentlicht in:	Biochemistry (Easton) 1992-03, Vol.31 (9), p.2576-2582
Hauptverfasser:	Macquaire, Francois, Baleux, Francoise, Giaccobi, Emmanuelle, Huynh Dinh Tam, Neumann, Jean Michel, Sanson, Alain
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Biological and medical sciences Chemical Phenomena Chemistry, Physical Deuterium effects on Fundamental and applied biological sciences. Psychology Glyceric Acids - chemistry Hydrogen-Ion Concentration interaction Interactions. Associations Intermolecular phenomena lipopeptides Lipoproteins - chemistry Magnetic Resonance Spectroscopy Micelles Molecular biophysics Molecular Sequence Data N.M.R Oligopeptides - chemical synthesis Oligopeptides - chemistry Palmitates - chemistry Phospholipids Phosphorylcholine - analogs & derivatives Protein Conformation Solutions structure
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