"Designability of Protein Structures"

Ned Wingreen,  NEC Research Institute, Princeton University

11:30 am, Friday 12 January 2001
Room 224 Physics-Astronomy Building, with refreshments at 11:15am.

This talk is jointly sponsored by the Campus Theory Seminar and by the Center for
Biological Modeling Seminar series.

Abstract:

The protein structures found in nature represent only a small fraction of all
possible folded configurations. A simple lattice model for protein folding has
helped identify a principle of "designability" which may explain the existence
of this preferred class. The highly designable structures, i.e. those which
are the ground states of a large number of sequences, have other protein-like
properties such as thermodynamic stability, fast folding, and geometrically
regular appearances. A mapping of the hydrophobic model onto a geometrical
representation explains both the origin of highly designable structures and
the close relation between designability and thermodynamic stability. Recent
work aims at the design of totally new protein structures.