Orientation of peptides in aqueous monolayer films. Infrared reflection-absorption spectroscopy studies of a synthetic amphipathic beta-sheet

Infrared reflection-absorption spectroscopy (IRRAS) intensities of the Amide I vibration are used to develop a quantitative approach for determining the Euler angles that describe the orientation of protein beta-sheets in aqueous monolayer films. A synthetic amphipathic peptide, Val-Glu-Val-Orn-Val-...

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Bibliographische Detailangaben
Veröffentlicht in:Langmuir : the ACS journal of surfaces and colloids. - 1992. - 20(2004), 9 vom: 27. Apr., Seite 3730-3
1. Verfasser: Xu, Zhi (VerfasserIn)
Weitere Verfasser: Brauner, Joseph W, Flach, Carol R, Mendelsohn, Richard
Format: Aufsatz
Sprache:English
Veröffentlicht: 2004
Zugriff auf das übergeordnete Werk:Langmuir : the ACS journal of surfaces and colloids
Schlagworte:Journal Article Research Support, N.I.H., Extramural Research Support, U.S. Gov't, P.H.S. Peptides
Beschreibung
Zusammenfassung:Infrared reflection-absorption spectroscopy (IRRAS) intensities of the Amide I vibration are used to develop a quantitative approach for determining the Euler angles that describe the orientation of protein beta-sheets in aqueous monolayer films. A synthetic amphipathic peptide, Val-Glu-Val-Orn-Val-Glu-Val-Orn-Val-Glu-Val-Orn-Val-OH is used as a test case. The pattern of Amide I frequencies suggests that the molecule is organized as an antiparallel beta-sheet at the air/water interface. The model used to simulate the Amide I intensities reveals that the beta-sheet has a slight preferential alignment parallel to the direction of compression; i.e., deviation from uniaxial symmetry is observed. In addition, the sheet is found to lie flat on the aqueous surface, with (presumably) the polar side chains interacting with the aqueous subphase. Limitations and advantages of the theoretical approach are discussed
Beschreibung:Date Completed 09.02.2006
Date Revised 26.10.2019
published: Print
Citation Status MEDLINE
ISSN:1520-5827