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Conformational properties of microtubule protein: Their relation to the self‐assembly process in vitro
Author(s) -
Bayley Peter M.,
Clark David C.,
Martin Stephen R.
Publication year - 1983
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360220114
Subject(s) - chemistry , tubulin , microtubule , dimer , oligomer , biophysics , in vitro , polymerization , kinetics , stereochemistry , crystallography , biochemistry , polymer chemistry , microbiology and biotechnology , organic chemistry , polymer , physics , quantum mechanics , biology
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 vitro . 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 self‐assembly. 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.