Conformation of lysozyme Langmuir monolayer studied by infrared reflection absorption spectroscopy

The surface chemistry and spectroscopy of the reduced lysozyme Langmuir monolayer were investigated at different pH values to compare with the native one. It was found that the limiting molecular area of the reduced lysozyme was not subphase pH dependent as the native lysozyme. To explain this resul...

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Veröffentlicht in:Langmuir : the ACS journal of surfaces and colloids. - 1991. - 25(2009), 5 vom: 03. März, Seite 2842-9
1. Verfasser: Thakur, Garima (VerfasserIn)
Weitere Verfasser: Leblanc, Roger M
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2009
Zugriff auf das übergeordnete Werk:Langmuir : the ACS journal of surfaces and colloids
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Peptides Water 059QF0KO0R Muramidase EC 3.2.1.17
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520 |a The surface chemistry and spectroscopy of the reduced lysozyme Langmuir monolayer were investigated at different pH values to compare with the native one. It was found that the limiting molecular area of the reduced lysozyme was not subphase pH dependent as the native lysozyme. To explain this result in terms of the conformation and orientation of the lysozyme Langmuir monolayer at various subphase pH values, we have used infrared reflection absorption spectroscopy. The interpretation of the results make plausible change of the conformation and orientation of the native lysozyme Langmuir monolayer with the subphase pH 3, 6, and 11 
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