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Future Work
We are starting to fully understand the ‘cofactor story’ as far as the
effect and
importance they have on restriction activity and complex formation. The introduction of fluor labelled DNA has made the process faster and safer to work with which means data can be collected collated and reproduced more accurately.
The molecular modelling predictions supplied by Janusz and those produced
by myself have started to provide the first structural information on any HsdR subunit. Although these models are only predictions and are very often wrong, they provide a testable hypothesis of a structure which has started to be backed by the limited proteolysis works and the AFM images which have begun to show a 3D structure of the protein for the first time in such high resolution.
The limited proteolysis so far has provided a lot of information about the
domain ‘make-up’ of HsdR and we are currently awaiting data obtained by tandem mass spectrometry, on proteolytic fragments isolated from an SDS-PAGE gel. This will allow us to determine the amino acid sequence of each fragment. structural differences and this work will be complemented with Scanning Tunnelling Microscopy (STM). which evidence is building to suggest is is highly flexible and therefore this will be a very challenging task. some seed crystals before the end of my studies. |
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