The primary focus of my research is PROTEINS; their expression, folding, stability, binding interactions and catalytic activities, as well as different aspects of the science, design and engineering associated with the study of their forms and functions.
My approach is a "many questions, many subjects, many systems, many techniques" type of approach. I prefer it to the single protein, single question, single system, single techniques type of approach. You could say that this is a personal preference. To understand proteins in as many different ways as possible, and from as many different angles as I possibly can, I explore the gamut of protein qualities and behaviors, using multi-pronged, multi-faceted approaches.
I also contribute to the development of methods, molecules, processes, and technologies relating to proteins, and to the training and tutoring of younger researchers, as well as to some research administration.
With proteins, the line dividing fundamental science from applications is very, very thin. My research group and I cross this line in both directions, quite often. About seventy-five percent of the work that we have done is already published or patented; the rest is in the pipeline.
You are welcome to explore this website and enjoy reading up on what we do.
This is a hypothesis paper. The propagation of prion proteins involves the hypothesis that a rogue prion protein molecule somehow turns other chemically-identical protein molecules (prions) into rogue molecules through a transformative process involving a change of alpha helical protein structures into beta sheet-based structures. In this paper, I showed through arguments how it was possible that rogue prion molecules interact with naïve B-cells in the mucosal associated lymphoid tissue in the gut, with the result that they are assessed by the immune system to be conformationally-foreign in respect of at least one structural epitope displayed on the rogue (scrapie) prion which is not displayed on the regular and native (cellular) prion. This was proposed to result in B-cell activation and proliferation, through largely T-independent mechanisms of B-cell activation, leading to the increased availability of immunoglobulins cognate to the rogue prion. Finally, it was suggested that the immunoglobulins cognate to the rogue prion act as chaperones that promote misfolding of cellular prion into rogue (scrapie) prion, by providing plaster-cast templates cognate to the rogue prion which induce freshly-synthesized prion to adopt the rogue (scrapie) conformation, by bleeding conformational equilibria away from the cellular conformation to the scrapie conformation. Some experimental evidence available at the time, to show the critical importance of availability of B-cells to prion propagation, was adduced to support the notion that prion propagation necessarily involves B-cells (and, therefore, probably) immunoglobulins cognate to the scapie form of the prion.
