Monday, 23 May 2005

This presentation is part of: Biological Chemistry Posters

The role of proline in the folding of alpha-conotoxins

H. Reyne Herold, Amy K. Croskey, and Balazs Hargittai. Saint Francis University, Loretto, PA

Evaluation of the significance of disulfide bridges is an important part of understanding the concept of protein folding. Our group is involved in determining how slight changes in the sequence of small peptides influence their folding properties. Our present studies focus on the folding of a group of multiple disulfide bridge containing small peptides, alpha-conotoxins SI, SIA, GI, GII and MI. These thirteen-fourteen amino acid containing peptide amides have two disulfide bridges leading to three possible regioisomers. Most reduced forms of native conotoxins are able to fold to form the natural isomer. However, under certain conditions the oxidation of these peptides yields this native isomer in a mixture of the other two isomers. This poster describes our results on the affects of different amino acids in some key position in the sequence of alpha-conotoxins and compares oxidation results obtained under folding and denaturing conditions.

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