Thermal transitions in the structure of tubulin - Environments of aromatic aminoacids

A. Mozo-Villarías, A. Morros, J. M. Andreu

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18 Citations (Scopus)

Abstract

The environment of aromatic aminoacids in the thermal transition of brain tubulin has been studied by several spectroscopic techniques (Fourth Derivative, Difference Absorption, Fluorescence and Circular Ditchroism), in order to study its denaturation. An irreversible, temperature-induced, structural transition was found at around 48°C. In order to establish the relative degree of hydrophobicity of tubulin aromatic residues, before and after the thermal transition, difference and fourth derivative absorption spectra at different temperatures were compared with spectra of tyrosine and tryptophan model compounds in different media. It was found that at high temperatures, tubulin acquires a partially denatured stable state, with a significant amount of residual structure still preserved. This state is characterized by a general increase of the exposure of tyrosine residues to the medium, while the environment of tryptophans becomes more hydrophobic. © 1991 Springer-Verlag.
Original languageEnglish
Pages (from-to)295-300
JournalEuropean Biophysics Journal
Volume19
Issue number6
DOIs
Publication statusPublished - 1 May 1991

Keywords

  • Circular dichroism
  • Difference absorption
  • Fluorescence
  • Fourth derivative spectrophotometry
  • Hydrophobicity
  • Structural transition
  • Thermal denaturation
  • Tubulin

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