B.S. (Bachelor of Science)
Department of Biological Sciences
Scorpion activator polypeptides specifically bind to sodium channels, however the mechanism of binding is unknown. A hypothesis has been advanced by my project mentor (Dr. R. Hahin) that specifies the part of the molecule that binds and interacts with the channel. Also, certain parts of the activators play a key role in the maintenance of its three dimensional structure. The focus of the project is to compare peptides to further test the hypothesis and obtain important structural information that may well be common to all the molecules. Studies and analysis were achieved by using bioinformatic tools such as NCBI, EMBO, RSCB, SWISS-PROT, and SDMC to locate toxins. Clustal W alignment program was used to perform a multiple sequence alignment of the peptides and Deepview was used to identify key structural regions. New information was gained about how activator peptides bind to and modify sodium channels. Important structural and sequence motifs of the molecules were also identified.
Sampson, Regina, "Structural comparison of scorpion activator peptides" (2007). Honors Capstones. 1054.
Northern Illinois University
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