Neutron Reflectometry of Membrane Protein Assemblies at the Solid/Liquid Interface
Stephen A. Holt A C , Jeremy H. Lakey B , Sofian M. Daud B and Neil Keegan BA ISIS, Rutherford Appleton Laboratory, CCLRC, Chilton, OX11 0QX, UK.
B School of Cell and Molecular Biosciences, University of Newcastle-upon-Tyne, NE2 4HH, UK.
C Corresponding author. Email: s.a.holt@rl.ac.uk
Australian Journal of Chemistry 58(9) 674-677 https://doi.org/10.1071/CH05112
Submitted: 12 May 2005 Accepted: 28 July 2005 Published: 21 September 2005
Abstract
Neutron reflectometry has been used to study the self-assembly of a membrane protein, OmpF, onto a gold-coated silicon substrate from solution. OmpF associates into trimers and has been modified so that each trimer binds to the gold substrate through cysteine residues. Quantitative analysis of the data revealed that 12% of the surface was covered by the oriented protein with 27600 water molecules surrounding each trimer.
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