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An Isaac Newton Institute Workshop

Protein-Protein Interactions in Vitro and in Vivo

Sequence patterning in simple de novo proteins with tailored association behavior

23rd June 2004

Author: James Harden (Johns Hopkins University)

Abstract

Patterning of charged or hydrophobic residues in repetitive amino acid sequences is often associated with the formation of well-defined assemblies such as helix bundles and beta sheets. In recent years, de novo protein designs have extensively utilized such patterned motifs to construct minimalist sequences that fold or aggregate in a predetermined manner via the specific association of secondary structures. This talk will discuss examples of de novo designs based on associating amphiphilic secondary structures. In particular, we will focus on a series of modular de novo proteins that preferentially form homo- and hetero-trimeric assemblies. The stability of these assemblies and the secondary structure of the associating elements in various solution conditions will be presented and discussed in the context of opportunities for theoretical models of these simple systems