Michael A. Hicks, Ph.D.
Current efforts in enzyme design indicate that engineering novel functions in a general fashion requires a greater understanding of protein structure-function relationships. By using advanced bioinformatic techniques in tandem with combinatorial experimental methods, we have begun to understand that there are inherent constraints on the catalytic functions that protein scaffolds can perform. It is therefore important to know what capabilities and constraints exist within a given protein template prior to attempting the design of novel function.
My research specifically focuses on elucidating the structural and catalytic strategies employed by six-bladed beta-propeller enzymes. Through phylogenetic and engineering efforts, I hope to better understand how nature has evolved activities within this fold class.
Ph.D. 2011, University of California, San Francisco
B.S. 2005, Biology, Wake Forest University
The evolution of function in strictosidine synthase-like proteins.
Hicks MA, Barber AE, Giddings L-A, Caldwell J, O'Connor SE, and Babbitt PC, Proteins: Structure, Function, and Bioinformatics, 79: 3082-3098 (2011).