J. Chem. Phys., 113, 5072-5077 (2000)
Compactness, aggregation, and prionlike behavior of protein: A lattice
model study
Gilberto Giugliarelli, Cristian Micheletti, R. Banavar and Amos Maritan
Link to online article.
ABSTRACT
The solubility and compactness of proteins is investigated
within the framework of models amenable to an exact numerical study
through exhaustive enumeration. We study how the average inter-amino
acid interaction potential affects the properties of both isolated and
interacting proteins. In a concentrated solution, depending on the
value of the average potential, individual proteins may remain stable
in the isolated native structure soluble case, may aggregate
preserving their geometrical shape nonsoluble case or aggregate
changing their geometrical shape prionlike behavior. The number of
sequences that have compact native states and are soluble is maximal
at a fine-tuned average interaction potential and of the same order of
the corresponding number of nonsoluble prionlike proteins. The viable
protein sequences selected by such a fine-tuned potential are found to
have an amino acid composition similar to naturally occurring
proteins.