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The Motility of Monomeric and Dimeric Variants of Eg5 studied in the Presence of the Kinesin-5-specific Inhibitor Monastrol

✍ Scribed by Lakämper, Stefan; Thiede, Christina; Reiter, Stefanie; von Roden, Kerstin; Schmidt, Christoph F.


Book ID
122206046
Publisher
Biophysical Society
Year
2009
Tongue
English
Weight
89 KB
Volume
96
Category
Article
ISSN
0006-3495

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X-Ray Structure, Conformational Analysis
✍ C.Oliver Kappe; Oleg V Shishkin; Georg Uray; Petra Verdino 📂 Article 📅 2000 🏛 Elsevier Science 🌐 French ⚖ 108 KB

The conformational features of the mitotic kinesin Eg5 inhibitor monastrol were investigated by computational (AM1, HF/3-21G ‫ء‬ ), X-ray diffraction, and NMR studies showing that monastrol is a conformationally highly flexible molecule. Racemic monastrol was resolved by direct enantioselective HPLC