2015 Student Research Conference:
28th Annual Student Research Conference

Inhibition of Kinesin Binding Activity by H12 Alpha Helix from the Beta Tubulin Protein
Ryan N. Weber
Dr. Vayujeet Gokhale, Faculty Mentor

Kinesins are molecular motors that are used in cellular processes such as mitosis and transporting cargos. Many diseases can arise when these motor driven processes malfunction. Inhibitors of kinesin motors are coveted for potential use in medicine as a way to combat these diseases. H12 is an alpha helix in the tubulin protein, which is exposed on the surface of microtubules. H12 has been determined to be the major active site in the binding of kinesin to microtubules. We have therefore used optical trapping in vitro to study the inhibition of KIF5A binding to microtubules by the H12 peptide. This study determined if KIF5A would bind to H12 alone and inhibits the binding activity of kinesin to microtubules or if the other less active binding sites in tubulin were required for kinesin to bind and also measured the degree at which H12 inhibits the binding activity.

Keywords: Kinesin, H12, Microtubules, Motor proteins, KIF5A


Presentation Type: Oral Paper

Session: 310-5
Location: MG 1096
Time: 2:00

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