Organick Lecture Series
David E. Shaw
Chief Scientist
D.E. Shaw Research
Center for Computational Biology and Bioinformatics, Columbia University
Monday, April 2, 2012
220 Skaggs Biology Building (ASB)
Reception 6:15 p.m.
Lecture 7:00 p.m.
Title: Watching Proteins Dance: Molecular Simulation and the Future of Drug Design
David E. Shaw
Chief Scientist
D.E. Shaw Research
Center for Computational Biology and Bioinformatics, Columbia University
Monday, April 2, 2012
220 Skaggs Biology Building (ASB)
Reception 6:15 p.m.
Lecture 7:00 p.m.
Title: Watching Proteins Dance: Molecular Simulation and the Future of Drug Design
Abstract
Most of the drugs currently used in the treatment of human disease are chemical compounds that attach themselves in a highly selective "lock-and-key" fashion to specifically targeted protein molecules within the body. This process of molecular binding typically induces changes in the structure, behavior, and/or function of the target protein, which can in turn exert various effects on other biological molecules. Although laboratory experiments have elucidated many aspects of the structural and dynamic characteristics of proteins, the ability to observe the motion and behavior of individual protein molecules at an atomic level of detail -- both in isolation and in their interactions with other molecules -- could in principle enable promising new approaches to the process of drug development. New computational techniques and technologies have recently made it possible to simulate the behavior of proteins and their molecular partners over a timescale on which many biologically critical phenomena take place. These advances have begun to provide new insights into the molecular underpinnings of various diseases and the manner in which they might be attacked.
Most of the drugs currently used in the treatment of human disease are chemical compounds that attach themselves in a highly selective "lock-and-key" fashion to specifically targeted protein molecules within the body. This process of molecular binding typically induces changes in the structure, behavior, and/or function of the target protein, which can in turn exert various effects on other biological molecules. Although laboratory experiments have elucidated many aspects of the structural and dynamic characteristics of proteins, the ability to observe the motion and behavior of individual protein molecules at an atomic level of detail -- both in isolation and in their interactions with other molecules -- could in principle enable promising new approaches to the process of drug development. New computational techniques and technologies have recently made it possible to simulate the behavior of proteins and their molecular partners over a timescale on which many biologically critical phenomena take place. These advances have begun to provide new insights into the molecular underpinnings of various diseases and the manner in which they might be attacked.