Conformational properties of microtubule protein: Their relation to the self-assembly process in vitro
✍ Scribed by Peter M. Bayley; David C. Clark; Stephen R. Martin
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1983
- Tongue
- English
- Weight
- 256 KB
- Volume
- 22
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
Near-and far-uv CD spectra of microtubule protein preparations have been examined to study the possible role of protein conformation in relation to the kinetics of the self-assembly of these proteins into microtubules in uitro. Although tubulin can form conformations with high helical content under apolar solution conditions, this transformation is apparently not involved in self-assembly. There is no major perturbation of tubulin near-uv CD by reagents and solution conditions favoring assembly. Thus, in these preparations, tubulin, as dimer and as oligomer with MAPS, is effectively in the conformation in which it undergoes selfassembly. This conclusion is consistent with a hybrid model of assembly of microtubule protein involving direct incorporation of oligomeric species as an alternative to the condensation polymerization of tubulin dimer as the exclusive assembly mechanism.