Phase separation of intrinsically disordered proteins is important for the formation of membraneless organelles or biomolecular condensates, which play key roles in the regulation of biochemical processes within cells. In this work, we investigated the phase separation of different sequences of a coarse-grained model for intrinsically disordered proteins and discovered a surprisingly rich phase behavior. We studied both the fraction of total hydrophobic parts and the distribution of hydrophobic parts. Not surprisingly, sequences with larger hydrophobic fractions showed conventional liquid–liquid phase separation. The location of the critical point was systematically influenced by the terminal beads of the sequence due to changes in interfacial composition and tension. For sequences with lower hydrophobicity, we observed not only conventional liquid–liquid phase separation but also re-entrant phase behavior in which the liquid phase density decreases at lower temperatures. For some sequences, we observed the formation of open phases consisting of aggregates, rather than a normal liquid. These aggregates had overall lower densities than the conventional liquid phases and exhibited complex geometries with large interconnected string-like or membrane-like clusters. Our findings suggest that minor alterations in the ordering of residues may lead to large changes in the phase behavior of the protein, a fact of significant potential relevance for biology.
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21 February 2020
Research Article|
February 19 2020
Model for disordered proteins with strongly sequence-dependent liquid phase behavior
Special Collection:
JCP Editors' Choice 2020
Antonia Statt
;
Antonia Statt
a)
1
Department of Chemical and Biological Engineering, Princeton University
, Princeton, New Jersey 08544, USA
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Helena Casademunt
;
Helena Casademunt
b)
2
Department of Physics, Princeton University
, Princeton, New Jersey 08544, USA
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Clifford P. Brangwynne
;
Clifford P. Brangwynne
1
Department of Chemical and Biological Engineering, Princeton University
, Princeton, New Jersey 08544, USA
3
Howard Hughes Medical Institute
, Chevy Chase, Maryland 20815, USA
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Athanassios Z. Panagiotopoulos
Athanassios Z. Panagiotopoulos
c)
1
Department of Chemical and Biological Engineering, Princeton University
, Princeton, New Jersey 08544, USA
c)Author to whom correspondence should be addressed: [email protected]
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a)
Present address: Materials Science and Engineering, Grainger College of Engineering, University of Illinois, Urbana-Champaign, IL 61801, USA.
b)
Present address: Department of Physics, Harvard University, Cambridge, MA 02138, USA.
c)Author to whom correspondence should be addressed: [email protected]
J. Chem. Phys. 152, 075101 (2020)
Article history
Received:
December 03 2019
Accepted:
January 30 2020
Citation
Antonia Statt, Helena Casademunt, Clifford P. Brangwynne, Athanassios Z. Panagiotopoulos; Model for disordered proteins with strongly sequence-dependent liquid phase behavior. J. Chem. Phys. 21 February 2020; 152 (7): 075101. https://doi.org/10.1063/1.5141095
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