Peptide-related alterations of membrane-associated water : deuterium solid-state NMR investigations of phosphatidylcholine membranes at different hydration levels
Copyright 2004 John Wiley & Sons, Ltd.
| Veröffentlicht in: | Magnetic resonance in chemistry : MRC. - 1985. - 42(2004), 2 vom: 15. Feb., Seite 155-61 |
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| Format: | Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2004
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| Zugriff auf das übergeordnete Werk: | Magnetic resonance in chemistry : MRC |
| Schlagworte: | Journal Article Research Support, Non-U.S. Gov't Liposomes Membranes, Artificial Nerve Tissue Proteins Peptides Phosphatidylcholines Sodium Channels Water 059QF0KO0R mehr... |
| Zusammenfassung: | Copyright 2004 John Wiley & Sons, Ltd. Deuterated water associated with oriented POPC bilayers was investigated before and after the addition of 2 mol% peptide. Membranes in the presences of antimicrobial-(LAH4), pore-forming- (the segments M2 of influenza A and S4 of the domain I of rat brain sodium channels) or lysine-containing model peptides (LAK1 and LAK3) were investigated by (2)H and proton-decoupled (31)P solid-state NMR. The NMR spectra were recorded as a function of hydration in the range between 15 and 93% relative humidity and of sample composition. In the presence of peptides an increased association of water is observed. A quantitative analysis suggests that the peptide-induced changes in the lipid bilayer packing have a significant effect on membrane-water association. The quadrupolar splittings of (2)H(2)O at a given degree of hydration indicate that the changes of the water deuterium order parameter are specific for the peptide sequence and the lipid composition |
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| Beschreibung: | Date Completed 22.03.2005 Date Revised 21.11.2013 published: Print Citation Status MEDLINE |
| ISSN: | 1097-458X |