Our current protocol yields over 99%pure tubulin while preserving its natural dynamics. This is essential for studying protein on its own and its interaction with its binding partners. Research on tubulin in the brain helps understand neuronal structure, connectivity, neuroplasticity, or even neurodegenerative diseases, and it aids in developing targeted brain therapies or drugs.
The study of tubulin interactions utilizes advanced methods such as X-ray crystallography, cryo-EM, and NMR spectroscopy. Among these, NMR uniquely captures tubulin's natural behavior in solution, and this is why it requires protein to remain in the original active state. Precise knowledge of tubulin dynamics can drive future developments by enabling more effective drug design for tubulin-related diseases.
For example, it will enhance the understanding of cell division and aiding in the neural therapies for cancer and neurodegenerative conditions. This insight allows for precise modulation of tubulin function, leading to improved therapeutic outcomes. Microtubules are crucial components of eukaryotic cytoskeleton involved in various cellular functions.
Despite their similar structure, tubulin proteins undergo post-translational modification forming the tubulin code that regulates their function, controls cellular function and homeostasis.
