ORGN 518 |
Engineering a rhodopsin protein mimic
| Rachael M. Crist, Chrysoula Vasileiou, Courtney Olmsted, Erika Mathes, Soheila Vaezeslami, James H Geiger, and Babak Borhan. Department of Chemistry, Michigan State University, 320 Department of Chemistry, East Lansing, MI 48824 |
Protein / substrate interactions govern many important biological events including enzymatic specificity, biological sensing and signal transduction. Wavelength regulation, as utilized by rhodopsin, is an extraordinary example of the power of protein /substrate interactions culminating in color vision. However, due to difficulties in handling and manipulating these membrane-bound proteins, insight into their precise mechanisms has been limited. To help understand the effects responsible for wavelength regulation, we opted to engineer a rhodopsin protein mimic. Human Cellular Retinoic Acid Binding Protein II (CRABPII) is a small soluble protein and does not suffer from the difficulties membrane-bound proteins possess. We have re-engineered CRABPII from a non-covalent retinoic acid binding protein to a retinal binding protein, which forms the pivotal protonated Schiff base necessary for wavelength regulation. Site-directed mutagenesis is ongoing to probe the effect of bulky and charged amino acids on the chromophore, i.e. wavelength regulation. |
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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
The 226th ACS National Meeting, New York, NY, September 7-11, 2003
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