CHED 811 |
| Multivalent interactions are important in a variety of biological processes. In an effort to better understand these recognition processes on a molecular level, chemists have used a variety of synthetically derived glycopolymers to mimic natural glycoprotein and glycolipid assemblies. We are using a biosynthetic approach to generate homogeneous and chemically well-defined glycopolymers based on the ankyrin repeat protein scaffold. Ankyrin repeat (AR) proteins are found in almost all species and mediate numerous cellular processes. The conserved structural motif consists of 33 amino acid residues that fold into a β-turn followed by two antiparallel α-helices. Repeats of this motif stack side-by-side to form domains that are stabilized by hydrophobic interactions between the helices. AR domains thus provide a simple and robust scaffold for biochemical studies. Recombinant AR protein was expressed in E. coli and purified to homogeneity by affinity chromatography. The protein is soluble and folded in solution as determined by 2D 1H-15N NMR. We have chemically modified the AR scaffold to display synthetic monosaccharides and are using these artificial glycoproteins to study the interaction between mannose and concanavalin A. |
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Undergraduate Research Poster Session: Biochemistry
2:00 PM-4:00 PM, Monday, April 7, 2008 Morial Convention Center -- Hall A, Poster
Division of Chemical Education |