Interaction of tubulin with phospholipid vesicles. II. Physical changes of the protein.

N. Kumar, R. D. Klausner, J. N. Weinstein, R. Blumenthal, M. Flavin

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25 Scopus citations


We have shown that soluble tubulin will bind to small unilamellar vesicles of dipalmitoyl phosphatidylcholine (Klausner, R. D., Kumar, N., Weinstein, J. N., Blumenthal, R., and Flavin, M. (1981) J. Biol. Chem. 256, 5879-5885). This association uniquely occurs at the lipid phase transition. The tubulin, when bound to the vesicles, displays an altered tryptophan fluorescence characterized by a 5-nm blue shift in the emission maximum and a 22% decrease in fluorescence intensity, when compared to soluble tubulin. Tryptophans in vesicle-bound tubulin are less accessible to the aqueous collisional quenchers, acrylamide and iodide, than in soluble tubulin. Circular dichroism studies reveal an increase in alpha-helical content of tubulin as a result of vesicle interaction. Proteolytic digestion by trypsin of vesicle bound tubulin is slower than of soluble tubulin. The beta subunit of tubulin is preferentially protected from trypsin by vesicle interaction. Furthermore, the pattern of tryptic cleavage products is altered by this interaction.

Original languageEnglish (US)
Pages (from-to)5886-5889
Number of pages4
JournalJournal of Biological Chemistry
Issue number11
StatePublished - Jun 10 1981

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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