Abstract

Microtubules, formed by the polymerization of alpha and beta tubulin heterodimers, play an essential role in cell division and motility. The disordered C-terminal tails of each tubulin monomer are major sites of tubulin regulation and, despite being flexible, appear to regulate tubulin interactions with its binding partners. To study the C-terminal we use nuclear magnetic resonance (NMR) spectroscopy which is an ideal tool to probe the dynamics and properties of small, disordered regions such as the C-terminal tubulin tails.

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