Discovery of Small Molecule Inhibitors that Interact with γ-Tubulin
Article first published online: 15 FEB 2012
© 2012 John Wiley & Sons A/S
Chemical Biology & Drug Design
Volume 79, Issue 5, pages 639–652, May 2012
How to Cite
Friesen, D. E., Barakat, K. H., Semenchenko, V., Perez-Pineiro, R., Fenske, B. W., Mane, J., Wishart, D. S. and Tuszynski, J. A. (2012), Discovery of Small Molecule Inhibitors that Interact with γ-Tubulin. Chemical Biology & Drug Design, 79: 639–652. doi: 10.1111/j.1747-0285.2012.01340.x
- Issue published online: 3 APR 2012
- Article first published online: 15 FEB 2012
- Accepted manuscript online: 23 JAN 2012 06:40AM EST
- Received 15 September 2011, revised 4 January 2012 and accepted for publication 7 January 2012
Figure S1. Human γ-tubulin construct sequence.
Figure S2. RMSD of the backbone atoms from the reference structure at the beginning of the MD simulation.
Figure S3. B-factors of the C atoms of the residues of γ-tubulin during the analyzed 16-24 ns period of the MD simulation.
Figure S4. Comparison of fluorescence quenching of colchicine to γ-tubulin and β-tubulin.
Figure S5. TUBG1/TUBB-TUBA dimer amine cross-linking with DSG (disuccinimidylglutarate).
Figure S6. Fluorescence quenching of two different batches of gamma-tubulin (A) old (B) new in the presence of colchicine under the same conditions reported in the manuscript.
Figure S7. Clustering analysis for the MD trajectory.
Figure S8. Dominant conformations of γ-tubulin in our MD trajectory.
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