When multiple macromolecular interactions sum together to give a tighter effective binding affinity, that effect is called avidity. Avidity as measured in protein engineering applications falls well short of the theoretical thermodynamic limit for the effect. I am investigating values of avidity in "natural" avidity contexts to determine how good avidity is when designed by nature. The results may reveal future design principles for protein engineering of avidity constructs, including therapeutic agents that legerage avidity to achieve high binding or multi-specificity.
Many proteins exist as homo-oligomers, meaning they bind other copies of themselves. Despite the importance of these interactions for protein function and stability, homo-oligomeric interactions in proteins are not well-studied. The homo-oligomeric state of most proteins in simple model organisms like S. cerevisiae or E. coli are not even known. I am working to determine the oligomeric state of a large number of proteins in S. cerevisiae.
Localizing two or more enzymes in a biochemical pathway has been shown to increase the rate of production of the biochemical product. Nature has designed systems, such as the carboxysome, to spatially localize enzymes in a pathway. I am working to build a quantitative model of this phenomenon.
© 2009- Curran Oi.