CHED 772 |
| Thioredoxin (Trx) belongs to a superfamily of proteins containing a redox-active disulfide bond, which functions in maintaining the reducing atmosphere of the cell. Trx's exhibit a strictly conserved motif of a -CXXC- amino acid sequence. Alteration of the variable amino acid residues in the conserved motif may alter the redox properties of Trx. The goal of this project was to generate a series of Trx variants containing one of either the acidic amino acids, glutamic acid and aspartic acid, or the basic amino acids, lysine and arginine, at the first variable amino acid residue in the conserved motif by site-directed mutagenesis. A control variant with amino acid residues similar in the conserved motif to the prototypical Escherichia coli Trx was also generated, using a recombinant archael Trx as a template. Extended study will involve the over-expression and purification of the variants and the effects of variation on the redox potential of the protein. |
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Undergraduate Research Poster Session: Biochemistry
2:00 PM-4:00 PM, Monday, April 7, 2008 Morial Convention Center -- Hall A, Poster
Division of Chemical Education |