Thu, Mar 6, 2014, 2:00 pm to 3:30 pm
Joseph Henry Room
Proteins are the nanometer-scale machines that perform most of the chemical and mechanical work within cells. Each protein is a polymer string that folds into a unique ground state structure that endows the protein with its unique functionality. I will show that despite their geometrical variability and structural heterogeneity, proteins conform to a set of quantitative rules. These rules are emergent and often surprising, governing maximum protein size, folding speed, and intra-protein communication efficiency. These rules clarify the fundamental issues (conformational entropy, metastability, and frustration/glassiness) facing robust protein folding, function, and self-assembly. Finally, I will demonstrate how this theoretical framework can be used to surmount current bottlenecks facing the fields of drug design, neurodegenerative diseases and viral infection.