ArticleProceedings of the National Academy of Sciences of the United States of America2008
Probing the origin of tubulin rigidity with molecular simulations.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- A Comprehensive Study on the Electrostatic Properties of Tubulin-Tubulin Complexes in Microtubules.Cells · 2023Article
- Atomistic molecular dynamics simulations of tubulin heterodimers explain the motion of a microtubule.European biophysics journal : EBJ · 2021Article
- Coarse-Grained Simulation of Mechanical Properties of Single Microtubules With Micrometer Length.Frontiers in molecular biosciences · 2020Article
- Maintenance of electrostatic stabilization in altered tubulin lateral contacts may facilitate formation of helical filaments in foraminifera.Scientific reports · 2016Article
- Are protein-protein interfaces special regions on a protein's surface?The Journal of chemical physics · 2015Article
- Molecular investigations into the mechanics of a muscle anchoring complex.Biophysical journal · 2015Article
- Tubulin bond energies and microtubule biomechanics determined from nanoindentation in silico.Journal of the American Chemical Society · 2014Article
- Structural transitions and energy landscape for Cowpea Chlorotic Mottle Virus capsid mechanics from nanomanipulation in vitro and in silico.Biophysical journal · 2013Article
- Mechanical transition from α-helical coiled coils to β-sheets in fibrin(ogen).Journal of the American Chemical Society · 2012Article
- Mechanism of fibrin(ogen) forced unfolding.Structure (London, England : 1993) · 2011Article
- Anisotropic elastic network modeling of entire microtubules.Biophysical journal · 2010Article
- Order statistics theory of unfolding of multimeric proteins.Biophysical journal · 2010Article
- Exploring the contribution of collective motions to the dynamics of forced-unfolding in tubulin.Biophysical journal · 2010Article
- Experimental and computational characterization of biological liquid crystals: a review of single-molecule bioassays.International journal of molecular sciences · 2009Review
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2 authors.
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Abstract
Tubulin heterodimers are the building blocks of microtubules, a major component of the cytoskeleton, whose mechanical properties are fundamental for the life of the cell. We uncover the microscopic origins of the mechanical response in microtubules by probing features of the energy landscape of the tubulin monomers and tubulin heterodimer. To elucidate the structures of the unfolding pathways and reveal the multiple unfolding routes, we performed simulations of a self-organized polymer (SOP) model of tubulin. The SOP representation, which is a coarse-grained description of chains, allows us to perform force-induced simulations at loading rates and time scales that closely match those used in single-molecule experiments. We show that the forced unfolding of each monomer involves a bifurcation in the pathways to the stretched state. After the unfolding of the C-term domain, the unraveling continues either from the N-term domain or from the middle domain, depending on the monomer and the pathway. In contrast to the unfolding complexity of the monomers, the dimer unfolds according to only one route corresponding to the unraveling of the C-term domain and part of the middle domain of beta-tubulin. We find that this surprising behavior is due to the viscoelastic properties of the interface between the monomers. We map precise features of the complex energy landscape of tubulin by surveying the structures of the various metastable intermediates, which, in the dimer case, are characterized only by changes in the beta-tubulin monomer.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.