Desmoplakin is a cytolinker protein vital to tissue exposed to shear forces, such as the skin and the heart. This thesis research combines three physical techniques for the study of desmoplakin, namely Nuclear Magnetic Resonance (NMR) Spectroscopy, Small Angle X-Ray Scattering (SAXS) and Atomic Force Microscopy (AFM). The structure of the desmoplakin linker domain (in the C terminal end) has been resolved by NMR spectroscopy, exhibiting an unprecedented fold that contains a pair of regular and irregular subdomains and whose monomeric state has been confirmed by SAXS. The desmoplakin plakin domain (in the N terminal end) immobilisation on a surface of graphite decorated with size-selected gold clusters (with 55 and 147 atoms) was studied by tapping mode AFM, which provided evidence of enhanced weak adsorption of the protein to the clusters. With the aim of improving the technique of immobilisation of single biological molecules with metal nanoparticles, a new technique of cluster immobilisation has been developed using small metal clusters (Au\(_2\)\(_0\)) to create channels in a graphite substrate. These channels function as defects on the surface of the graphite to anchor soft-landed clusters with the potential to bind the biomolecules.
| Identifer | oai:union.ndltd.org:bl.uk/oai:ethos.bl.uk:589712 |
| Date | January 2014 |
| Creators | Rodriguez Zamora, Penelope |
| Publisher | University of Birmingham |
| Source Sets | Ethos UK |
| Detected Language | English |
| Type | Electronic Thesis or Dissertation |
| Source | http://etheses.bham.ac.uk//id/eprint/4807/ |
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