Prof. Dmitry Matyushov
Department of Chemistry & Biochemistry
Arizona State University
Tempe, AZ

Monday, November 4, 2013
3:00 pm (CT)
3269 Beckman Institute

Abstract

The interface between a protein and hydration water is heterogeneous, both dynamically and statistically. The structure of interface affects the electrostatics at protein's active site and rates of chemical reactions carried by enzymes and redox proteins. I will cover recent results addressing the following questions: (i) Does the interfacial biological water produce electrostatic signatures specific to proteins? (ii) What is the spectrum of interfacial electrostatic fluctuations? (iii) How is protein-mediated chemistry affected by electrostatics? These questions touch on the fundamental issue of whether thermodynamics or dynamics drive the optimization of biology's performance. Our results show that tuning of biological machines is achieved by adjusting reaction time-scales to the spectrum of relaxation times of the protein-water thermal bath. Ergodicity is often dramatically broken in such systems. The departure from the canonical ensemble is used to optimize the efficiency.