Greetings!

 Nobel Laureate Lecture: Michael Levitt

What:
"Birth & Future of Multi-scale Modeling of Macromolecules"

Who:
2013 Nobel Laureate Michael Levitt
Professor of Structural Biology, Stanford University

When:
November 24, 2014, 4:30–6pm
Reception from 4:30–5pm, lecture starts at 5pm

Where:
GT Student Center Ballroom
Click here for directions

Sponsored by:
Georgia Tech's College of Computing and College of Sciences 
and Conexx: America Israel Business Connector

Register:
Click here to RSVP

 Abstract

The development multiscale models for complex chemical systems began in 1967 with publications by Warshel and Levitt recently recognized by the 2013 Nobel Committee for Chemistry. The simplifications used then at the dawn of the age of computational structural biology were mandated by computers that were almost a billion times less cost-effective than those we use today. These same multiscale models have become increasingly popular in application that range from simulation of atomic protein motion, to protein folding and explanation of enzyme catalysis. In this talk I describe the origins of computational structural biology and then go on to show some of the most exciting current and future applications.

 Biography

Michael Levitt is an American-British-Israeli biophysicist and professor of structural biology in the Stanford University School of Medicine and a winner of the 2013 Nobel Prize in Chemistry. Born in South Africa in 1947, Levitt earned his Bachelor of Science in Physics from Kings College London and his Ph.D. in biophysics from Cambridge University. His research involves multi-scale approaches to molecular modeling: Coarse-grained models that merge atoms to allow folding simulation and hybrid models that combine classical and quantum mechanics to explain how enzymes works by electrostatic strain. Levitt's diverse interests have included RNA and DNA modeling, protein folding simulation, classification of protein folds and protein geometry, antibody modeling, x-ray refinement, antibody humanization, side-chain geometry, torsional normal mode, molecular dynamics in solution, secondary structure prediction, aromatic hydrogen bonds, structure databases, and mass spectrometry. His Stanford research team currently works on protein evolution, the crystallographic phase problem and Cryo-EM refinement. He is a member of both the Royal Society of London and the U.S. National Academy of Science. Levitt also remains an active computer programmer--"a craft skill of which I am particularly proud," he says.

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