Metastability of microtubules induced by competing internal forces

Viktória Hunyadi, Imre M. Jánosi

Research output: Article

11 Citations (Scopus)

Abstract

Recent modeling efforts to estimate energies of tubulin-tubulin bonds shed light on a delicate balance between competing mechanical forces maintaining microtubule walls. Here we formulate two important refinements to the explanation of bond energetics. First, energy surface calculations in the elastic filament approximation reveal a finite stabilizing barrier assumed a simple Lennard-Jones-like potential for protein bonds. The presence of a guanosine triphosphate (GTP) cap represented by straight segments is necessary, as it is predicted for a long time. In the lack of such a cap, the protofilaments are either in an absolutely stable or absolutely unstable state. Second, our calculations show that this barrier appears only if the mechanical energy associated with the conformational change after GTP hydrolysis (curling energy) is larger than the strength of lateral bonds. The overall energy balance we propose supports continuous assembly of GTP dimers, a metastable state in the presence of a finite GTP cap and energetically driven disassembly of guanosine diphosphate protofilaments.

Original languageEnglish
Pages (from-to)3092-3097
Number of pages6
JournalBiophysical journal
Volume92
Issue number9
DOIs
Publication statusPublished - máj. 2007

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ASJC Scopus subject areas

  • Biophysics

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