ORGN 517 |
| Chrysoula Vasileiou, Rachael Crist, Montserrat Rabago-Smith, and Babak Borhan. Department of Chemistry, Michigan State University, MSU, Chemistry Dep, Lansing, MI 48824 |
| Human Cellular Retinoic Acid Binding Protein II (CRABPII) has been modified to a retinal binding protein in an attempt to mimic rhodopsin and probe the effects responsible for wavelength regulation. The design of the protein’s cavity was such that an appropriately placed lysine residue can bind with the incoming aldehydic chromophore. This is predicated on appropriate design features to lower the pKa of the active site lysine residue for nucleophilic attack of retinal. Our efforts have been focused on verifying the nature of this substrate/protein interaction, i.e. non-covalent or Schiff base through a series of reductive amination studies. Overall, several spectroscopic techniques including UV, fluorescence, and MALDI-TOF have been applied towards elucidating the nature of this interation. In addition, attempts to determine the pKa of the engineered Lys by using specifically labeled proteins obtained through chemical ligation procedures coupled with NMR techniques will be discussed. |
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Bioorganic, Molecular Recognition, Asymmetric Reactions and Syntheses
11:00 AM-1:00 PM, Wednesday, September 10, 2003 Javits Convention Center -- Hall 1B/1C, Poster
Division of Organic Chemistry |