Microtubules (MTs) are pervasive throughout the cell and serve as one of the main structural components. In addition, MTs facilitate vital cell machinery, such as the dynamic mitotic spindle during division, and act as tracks for molecular motor protein transport. MTs are made up of polymerized alpha and beta tubulin dimers whose c-terminal tails, or E-hooks, extend from the MT surface, available for interaction with their surroundings. The negatively-charged E-hook has been shown to promote protein affinity, likely through strong, electrostatic interactions. Absence of the E-hook by experimental cleavage reduces bond lifetimes and motor protein processivity. However, E-hook structure and the environment's influence on its conformation is not well understood, especially considering the high potential for hydrogen bonding in physiological conditions. Here, we employ Raman spectroscopy and solvation techniques to elucidate the structure of the E-hook and the importance of hydrogen bonding in its role as a protein recruiter in the cell.

Spectroscopic characterization of the tubulin E-hook: Implications of protein affinity for microtubules

2019 Spring National Meeting

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