Conclusions

It has been shown that DPI offers an analytical technique to provide information on the orientation and structure of proteins in real time. The technique relies on classical optics, which are well understood, and provides dimensional information to a very high resolution (typically better than 0.01 nm) and mass loadings to a resolution of around 100 fg mm-2. It is possible not only to detect interactions between large proteins and small molecules, but also to quantify them and to determine stoichiometries. The technique described is not limited to the present measurement of thickness and refractive index of thin (protein) films, but has the potential to be extended to provide yet more detailed information relating to protein orientation and structure.

Acknowledgements. I would like to thank Professor David Fernig (Liverpool University), Dr. David Cullen, Dr. Kal Karim, Dr. Judith Taylor (Cran-field University), Professor Jian Lu (Manchester University) and Dr. Janos Voeroes (ETH Zurich) for their experimental expertise. I also gratefully acknowledge the experimental skills and diligence of Dr. Marcus Swann, Dr. Jonathan Popplewell and Dr. Louise Peel (Farfield Scientific) who undertook most of the experiments I have described. I would also like to Dr. Gerry Ronan (Farfield Scientific) and Dr. Marcus Swann for helpful discussions on the most appropriate ways to describe some of the physical concepts utilised by DPI. I would also thank Joanna Mosiezny (Farfield Scientific) for her patience and tenacity in preparing this document.

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