Difference between revisions of "Team:BostonU/Temporal Control/Workflow"

Revision as of 23:09, 18 September 2015

Our Workflow

There are various post-translational protein control methods that are known in the literature. Some of these include incorporation of an allosteric binding domain to disrupt protein structure and spatial sequestration of a protein to certain regions of a cell. We focused on a method known as conditional dimerization to control protein activity.

Naturally, proteins contain different domains that work together to carry out their overall function in the cell. Conditional dimerization involves splitting a protein by separately encoding both halves; this introduces physical separation of some functional domains and eliminates protein activity. Each encoded protein fragment is fused to an additional protein domain called a dimerization domain. These domains naturally bind in the presence of an inducer, which physically brings together the protein fragments to restore protein activity.

Some other specific advantages of conditional dimerization include:

It is only necessary to know the primary sequence of a protein to develop a conditional dimerization system. The protein can be split at any particular location between adjacent amino acids. Read about our modeling efforts to determine promising split locations.
There are several natural dimerization domains that are available in the literature. Read more about our dimerization domain choices.

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