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Non-natural amino acids are additional to the 20 naturally occurring amino acids that are used in ordinary protein synthesis. 3,4- dihydroxyphenylalanine (L-DOPA) is one such non-natural amino acid that has electrochemical properties. By globally incorporating L-DOPA into glucose binding protein (GBP), glucose can be electrochemically detected based on the hinge motion of the binding pocket of GBP in the presence of L-DOPA. L-DOPA was successfully expressed and purified in a phenylalanine auxotroph, GBP152-PheL-DOPA, but not successfully expressed in a tyrosine auxotroph. Cyclic voltammetry was used and the data obtained indicated that an increase in glucose concentration corresponded to a decrease in oxidation, meaning that L-DOPA is less readily oxidized to the quinone structure in the presence of glucose. This data is in agreement that L-DOPA is involved in, and stabilized by, binding of glucose in GBP152-PheL-DOPA.
Cullinan, Megan, "Design of an Electroactive Glucose Binding Protein Variant Using Global Incorporation of Non-Natural Amino Acids" (2016). Fall Interdisciplinary Research Symposium. Paper 16.
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