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Persistent URL http://purl.org/net/epubs/work/34152
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Record Id 34152
Title Neutron reflectometry of membrane protein assemblies at the solid/liquid interface
Abstract Neutron reflectometry has been used to study each step in the self-assembly of a membrane protein, OmpF, onto a gold coated silicon substrate from solution. The OmpF associates into trimers and has been modified so that each trimer contains three cysteines which bind to the gold substrate. Quantitative analysis of the data revealed that 10 % of the surface was covered by the oriented protein with 43,000 water molecules surrounding each trimer. Deposition of lipids around the trimers allowed a model membrane structure to be achieved and qualitatively analysed with further development required to fully analyse this complex system.
Organisation CCLRC , ISIS , SURF
Keywords Biology , Protein , Self assembly , Neutron Reflectometry , ISIS 2005
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Language English (EN)
Type Details URI(s) Local file(s) Year
Journal Article Aus J Chem 58, no. 9 (2005): 674-677. doi:10.1071/CH05112 2005
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