Mechanochemical action of the dynamin protein

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dc.creatorLenz, Martin
dc.creatorProst, Jacques
dc.creatorJoanny, Jean-François
dc.date2008-04-05
dc.date2008-06-18
dc.date.accessioned2026-07-07T09:56:58Z
dc.date.available2026-07-07T09:56:58Z
dc.descriptionDynamin is a ubiquitous GTPase that tubulates lipid bilayers and is implicated in many membrane severing processes in eukaryotic cells. Setting the grounds for a better understanding of this biological function, we develop a generalized hydrodynamics description of the conformational change of large dynamin-membrane tubes taking into account GTP consumption as a free energy source. On observable time scales, dissipation is dominated by an effective dynamin/membrane friction and the deformation field of the tube has a simple diffusive behavior, which could be tested experimentally. A more involved, semi-microscopic model yields complete predictions for the dynamics of the tube and possibly accounts for contradictory experimental results concerning its change of conformation as well as for plectonemic supercoiling.
dc.description17 pages, 4 figures; typos corrected, reference added
dc.identifierhttps://arxiv.org/abs/0804.0859
dc.identifierhttp://arxiv.org/abs/0804.0859
dc.identifierPhys. Rev. E 78, 011911 (2008) and Virtual Journal of Biological Physics Research 16, 3 (2008)
dc.identifierdoi:10.1103/PhysRevE.78.011911
dc.identifier.urihttp://salesiana.dossiersoluciones.com/handle/123456789/167173
dc.subjectSoft Condensed Matter
dc.subjectBiological Physics
dc.subjectBiomolecules
dc.titleMechanochemical action of the dynamin protein
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