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Protein Engineering, Vol. 12, No. 9, 721-726, September 1999
© 1999 Oxford University Press

The evolutionary landscape of functional model proteins

Jonathan D. Hirst

Department of Molecular Biology, TPC-6, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA

To study the distinct influences of structure and function on evolution, we propose a minimalist model for proteins with binding pockets, called functional model proteins, based on a shifted-HP model on a two-dimensional square lattice. These model proteins are not maximally compact and contain an empty lattice site surrounded by at least three nearest neighbors, thus providing a binding pocket. Functional model proteins possess a unique native state, cooperative folding and tolerance to mutation. Due to the explicit functionality in these models (by design), we have been able to explore their fitness or evolutionary landscapes, as characterized by the size and distribution of homologous families and by the complexity of the inter-relatedness of the functional model proteins. Mindful that these minimalist models are highly idealized and two-dimensional, functional model proteins should nevertheless provide a useful means for exploring the constraints of maintaining structure and function on the evolution of proteins.

Keywords: binding pocket/evolution/HP model/non-compact/protein


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