8:30 AM-9:15 AM
New Hampshire Ballroom
Chair: Rolf Jeltsch, ETH-Zentrum, Switzerland
Protein folding is one of the most fundamental processes in all living matter and concerns the transition of a disordered chemical chain of amino acid residues into a precisely ordered three-dimensional folded structure that is then able to carry out all the key biological functions.
The process is a closed problem in that the particular amino acid sequence to lead to a particular folded shape. It is complicated by the large number of degrees of freedom that characterize a protein chain as well as our inexact knowledge of all the physical forces responsible for the stability of the folded state.
By looking at the problem from different viewpoints including experimental, physical, biological, mathematical, algorithmic and computational, we gain insight that has led to some success in blind predictions of structure from sequence.For more details, please consult the author's web page at: http://csb.stanford.edu/levitt
Department of Structural Biology
Stanford Medical School, USA