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Date of Award
Restricted Thesis: Campus only access
Bachelor of Science
Dr. Lisa Gentile
Kinesin is a motor protein that uses ATP to transport macromolecules along microtubules in the cell. It is a heterotetramer composed of two heavy chains, which walk along the microtubule, and two light chains, which are involved with cargo binding. The research described here focuses on the kinesin light chains (KLCs), which have been suggested to contain six tetratrico peptide repeats (TPRs). Each TPR has a 34 amino acid sequence and is predicted to form a helix-loop-helix motif. To experimentally determine if these TPRs form the expected secondary structure, KLC TPRs 1, 1-2, and 1-5 were isolated and characterized as fusion proteins with MBP. Separation of the KLC TPRs from MBP was attempted using genenase before isolating and characterizing KLC TPR 1-5 through direct expression. Results are presented that suggest KLC has α-helical secondary structure, consistent with it being a TPR protein.
Weck, Meredith, "Characterization of the secondary structure of kinesin light chain tetraticopeptide repeats" (2010). Honors Theses. 146.