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Relation between single-molecule properties and phase behavior of intrinsically disordered proteins
Open accessAbstract
Significance: Some proteins can undergo phase separation in vivo to form membraneless organelles with distinct physiological functions. In many cases, the driving force is believed to be the intrinsically disordered domains that lack regular structural features and can phase separate in vitro. Relating protein sequences to phase-separation propensity is the goal of this work. Toward this goal, we highlight the connection between the temperature where a single chain collapses, the temperature where interactions within a dilute solution favor self-association, and the critical temperature of phase separation. Our results show that these characteristic temperatures are highly correlated, suggesting that experiments performed in dilute conditions may be used to predict phase separation.
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Cites
Fast Parallel Algorithms for Short-Range Molecular Dynamics
Plimpton, S. (1995) · Journal of Computational Physics · doi:10.1006/jcph.1995.1039 · Cited by 44,721
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Schuler, B., Borgia, A., Borgia, M. B., Heidarsson, P. O., Holmstrom, E. D., Nettels, D., & Sottini, A. (2020) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2019.12.006 · Cited by 91
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Minimal coarse-grained models for molecular self-organisation in biology
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Metadata
- Authors
- Dignon, G. L., Zheng, W., Best, R. B., Kim, Y. C., & Mittal, J.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2018-09-14
- Volume
- 115
- Issue
- 40
- Pages
- 9929-9934
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2891753890
- Cited by
- 409
- References
- 1
- FWCI
- 9.89
- Type
- journal article
- Language
- en
- Open access
- green
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- Dignon, G. L., Zheng, W., Best, R. B., Kim, Y. C., & Mittal, J. (2018). Relation between single-molecule properties and phase behavior of intrinsically disordered proteins. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.1804177115
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