Faculty Research

Dr. Nick Panasik

Associate Professor
Department of Biology
James S. Thomas, 221 
Email: npanasik@claflin.edu
Phone: (803) 535-5535
Fx: (803) 535-5776

webpage: Dr. Panasik


The a/b barrel (TIM) enzyme fold is the largest family of protein folds (representing at least 10% of all known protein structures) and has the widest range of enzyme functions. My research focuses on elucidating the structural basis for folding specificity and thermodynamic stability in this class of enzymes and the future application of those principles in protein design.  My past work using directed evolution techniques and crystallographic analysis has led to the proposal of specific determinants of protein stability in this class of enzymes. In my current research, I use random PCR mutagenesis to create libraries of genetic variants for low or high temperature adapted beta-galactosidases (for treatment of lactose intolerance), cellulases (bio fuel related enzymes), and bacterial luciferases (temperature biosensors) and study the effect of such mutations on protein structure. Using ab initio Monte Carlo simulations, estimations of the contribution of steric exclusion to main chain and side chain entropy are made that lead to identification of new classes of substitutions and novel models of protein thermostabilization through entropy.