Biopolymers have many fascinating properties coming from a competition betw
een universal features, well known in the physics of synthetic polymers, an
d specific elements which are crucial for the biological function of these
molecules. Proteins are an example of this richness: proteins are heteropol
ymers consisting of hydrophobic and hydrophilic segments, and carry charges
of both signs along the backbone. Simple models of such heteropolymers hav
e been studied in connection with the folding and evolution of proteins. Ho
wever, these models can only give a limited understanding of real proteins,
and elements specific to proteins must be included. Our approach to this p
roblem has been to construct a model of the specific self-interactions of p
roteins by defining a unique folding pathway. This model reproduces the the
rmodynamic properties of proteins. (C) 2000 Elsevier Science B.V. All right
s reserved.