Leibly, David J. (2013 - 2016)
David is in the Department of Chemistry and Biochemistry. He joined the training program in 2013. His research mentor is Dr. Todd Yeates. He received a B.S. degree in 2009 from U. Washington.
Mentor: Dr. Todd Yeates
Determination of the three-dimensional structure of proteins can answer questions on how the protein recognizes a substrate, it may reveal unique structural features that may be targets of novel therapeutics and, perhaps most importantly, provide a structure that presents a new set of questions to be explored. However, upwards of 70% of proteins will fail to crystalize. By utilizing a synthetic symmetrization, via a series of pre-formed GFP dimers we hope to improve the crystallization rates of difficult to crystalize proteins. With our approach, we will create a non-covalent fusion between GFP dimers and an asymmetric crystallization target. This in turn, will induce synthetic symmetry of the crystallization target. This method will allow the exploration of distinct crystal lattice possibilities for each GFP dimer used, increasing the possibility of crystal formation.
