Department of Chemistry and Biochemistry Seminar
- Friday, March 9, 2018 at 3:10pm
- Chemistry and Biochemistry Building, Byker Auditorium - view map
Dr. Pratyush Tiwary from the Department of Chemistry & Biochemistry and Institute for Physical Science & Technology University of Maryland, College Park will present "Designing Dynamical Maps of Molecular Systems with Statistical Mechanics and Predictive Artificial Intelligence."
Anyone who has ever gotten stuck in traffic knows how the superiority of a GPS-based map or app over a traditional print map comes not necessarily just from the former’s access to more information, but more so its access to dynamical information, for e.g. the flow of traffic. Similarly, in the last decade, a consensus view is emerging that we should not view proteins, and materials in general, as static entities but instead account for their ever-fluctuating dynamic nature. In this talk, we will describe how we are trying to amalgamate traditional statistical mechanics with recent developments in predictive artificial intelligence (AI) and deep learning to construct and use “dynamical maps” for molecular systems. These low-dimensional dynamical maps go beyond traditional static molecular maps (also called potential or free energy landscapes) by incorporating information also about dynamic quantifiables. We will then illustrate their usefulness with the fundamentally important problem of drug unbinding from proteins. A very important feature of drug efficacy is the drug’s residence time in the target protein. Structural details of the unbinding process are in general hard to capture in experiments, while the relevant timescales are far beyond the most powerful supercomputers. Here we will show how by constructing appropriate dynamical maps we are able to elucidate with unprecedented spatio-temporal resolution and statistical reliability the entire unbinding process of a variety of ligand-protein systems, shedding light on the role of protein conformations and of water molecules as molecular determinants of unbinding.
- Department of Chemistry and Biochemistry