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Full Record Details
Persistent URL
http://purl.org/net/epubs/work/34152
Record Status
Checked
Record Id
34152
Title
Neutron reflectometry of membrane protein assemblies at the solid/liquid interface
Contributors
SA Holt (CCLRC Rutherford Appleton Lab.)
,
JH Lakey
,
SM Daud
,
N Keegan
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
,
ISIS-SURF
Keywords
Funding Information
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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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