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Condensation Agents Determine the Temperature–Pressure Stability of F‐Actin Bundles
Author(s) -
Gao Mimi,
Berghaus Melanie,
von der Ecken Julian,
Raunser Stefan,
Winter Roland
Publication year - 2015
Publication title -
angewandte chemie
Language(s) - English
Resource type - Journals
eISSN - 1521-3757
pISSN - 0044-8249
DOI - 10.1002/ange.201504247
Subject(s) - fascin , actin , dissociation (chemistry) , solvation , chemical physics , chemistry , biophysics , condensation , chemical engineering , crystallography , materials science , nanotechnology , thermodynamics , molecule , physics , organic chemistry , biochemistry , biology , engineering
Biological cells provide a large variety of rodlike filaments, including filamentous actin (F‐actin), which can form meshworks and bundles. One key question remaining in the characterization of such network structures revolves around the temperature and pressure stabilities of these architectures as a way to understand why cells actively use proteins for forming them. The packing properties of F‐actin in fascin‐ and Mg 2+ ‐induced bundles are compared, and significantly different pressure‐temperature stabilities are observed because of marked differences in their nature of interaction, solvation, and packing efficiency. Moreover, differences are observed in their morphologies and disintegration scenarios. The pressure‐induced dissociation of the actin bundles is reminiscent of a single unbinding transition as observed in other soft elastic manifolds.