Past Undergraduate Researchers
- Derek Danner
- Rachel Landgren
- Danielle Roberts
- Colin Wiley
- Gus Wilson
- Thomas Rainbolt
Hollenbeck Research Group
Protein-carbohydrate interactions are important in a variety of biological processes, including viral entry, cell surface adhesion, and fertilization. Yet the affinity of one carbohydrate for one protein is remarkably low (Kd ~ 1 mM). Proteins circumvent this problem by binding to multiple carbohydrate residues simultaneously forming a multivalent complex with high affinity. Our research involves the design and synthesis of new materials to study these types of interactions in biological systems.
The ankyrin repeat (AR) is one of the most common protein sequence motifs. AR proteins are composed of tandem repeats of ca. 33 amino acid residues that form a b-turn followed by two antiparallel a-helices (see below). These repeats stack together to form an elongated structure ideally suited for the presentation of multiple functional groups and/or recognition elements (e.g., monosaccharides) in a multivalent fashion.
Using a combination of biochemistry, molecular biology, and organic chemistry, students in my lab generate a series of ligands based on the ankyrin repeat protein scaffold and monitor binding of these ligands to a protein called concanavalin A (Con A). ConA is able to agglutinate cells (i.e., cause them to clump together) through multivalent interactions with cell surface carbohydrates. We believe that our ligands will prove to be both novel and effective inhibitors of this process.
Applicants must adhere to Chemistry department procedures and deadlines.
Qualifications of successful applicants
Qualified students will have a genuine interest in learning about scientific research and will have successfully completed CHEM 1318 and CHEM 2319 before the summer of 2010. No prior research experience is required.
