CHED 561 |
| Small molecules that resemble beta-sheets may be capable of mimicking the behavior of naturally occurring beta-sheets without the added complexity of the protein in its entirety. These small molecules have become important tools in understanding molecular recognition, protein-protein interactions and protein folding. A cystine dimer is a simple and easily created molecule that exhibits such a structure. The disulfide bond between the cystines functions as an effective scaffold for hydrogen bond formation that is consistent with beta-sheet secondary structure. Extension of the peptide strands to increase the number of hydrogen bonds produces a structure that more closely resembles naturally occurring beta-sheets. |
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Undergraduate Research Poster Session: Organic Chemistry
11:00 AM-1:00 PM, Monday, March 26, 2007 Hyatt Regency Chicago -- Riverside Center, Poster
Division of Chemical Education |