Understanding protein structure, function and dynamics ranks among the most
challenging and fascinating problems faced by science today. Since the function
of a protein is related to its three dimensional structure,
manipulation of the latter by means of mutation in the protein sequence
generates functional diversity. The keys that will help us understand
this mechanism and consequently protein sequence evolution lie in the yet
unknown laws that govern protein folding. The knowledge of these laws would
also prove useful for engineering protein molecules to optimize their
activities as well as to alter their pharmacokinetic properties in the case of
therapeutically important molecules. I am particularly interested in
developing new numerical and computational approaches to the
protein design problem (also called inverse folding problem),
using fundamental ideas from physics and mathematics.
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