SISSA - Basement floor - room A

********************************************************************

Abstract:

We present the simple coarse-grained model which demonstrates that the
native folds of proteins can emerge on the basis of their common
attributes. These are the inherent anisotropy of the chain molecule, the
geometrical and energetical constraints imposed by hydrogen bonding,
sterics and hydrophobicity. Our study of homopolymers points to a
hypothesis that protein structures lie in a marginally compact phase in
which the free energy landscape is pre-sculpted by geometry and symmetry.
We elucidate the key role played by sequence design in selecting the
structure of choice from the predetermined menu of putative native state
structures, and the tendency of many chains to form amyloid aggregates