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Connecting Coil-to-Globule Transitions to Full Phase Diagrams for Intrinsically Disordered Proteins.

Publication ,  Journal Article
Zeng, X; Holehouse, AS; Chilkoti, A; Mittag, T; Pappu, RV
Published in: Biophysical journal
July 2020

Phase separation is thought to underlie spatial and temporal organization that is required for controlling biochemical reactions in cells. Multivalence of interaction motifs, also known as stickers, is a defining feature of proteins that drive phase separation. Intrinsically disordered proteins with stickers uniformly distributed along the linear sequence can serve as scaffold molecules that drive phase separation. The sequence-intrinsic contributions of disordered proteins to phase separation can be discerned by computing or measuring sequence-specific phase diagrams. These help to delineate the combinations of protein concentration and a suitable control parameter, such as temperature, that support phase separation. Here, we present an approach that combines detailed simulations with a numerical adaptation of an analytical Gaussian cluster theory to enable the calculation of sequence-specific phase diagrams. Our approach leverages the known equivalence between the driving forces for single-chain collapse in dilute solutions and the driving forces for phase separation in concentrated solutions. We demonstrate the application of the theory-aided computations through calculation of phase diagrams for a set of archetypal intrinsically disordered low-complexity domains. We also leverage theories to compute sequence-specific percolation lines and thereby provide a thermodynamic framework for hardening transitions that have been observed for many biomolecular condensates.

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Published In

Biophysical journal

DOI

EISSN

1542-0086

ISSN

0006-3495

Publication Date

July 2020

Volume

119

Issue

2

Start / End Page

402 / 418

Related Subject Headings

  • Thermodynamics
  • Temperature
  • Phase Transition
  • Intrinsically Disordered Proteins
  • Biophysics
  • 51 Physical sciences
  • 34 Chemical sciences
  • 31 Biological sciences
  • 06 Biological Sciences
  • 03 Chemical Sciences
 

Citation

APA
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ICMJE
MLA
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Zeng, X., Holehouse, A. S., Chilkoti, A., Mittag, T., & Pappu, R. V. (2020). Connecting Coil-to-Globule Transitions to Full Phase Diagrams for Intrinsically Disordered Proteins. Biophysical Journal, 119(2), 402–418. https://doi.org/10.1016/j.bpj.2020.06.014
Zeng, Xiangze, Alex S. Holehouse, Ashutosh Chilkoti, Tanja Mittag, and Rohit V. Pappu. “Connecting Coil-to-Globule Transitions to Full Phase Diagrams for Intrinsically Disordered Proteins.Biophysical Journal 119, no. 2 (July 2020): 402–18. https://doi.org/10.1016/j.bpj.2020.06.014.
Zeng X, Holehouse AS, Chilkoti A, Mittag T, Pappu RV. Connecting Coil-to-Globule Transitions to Full Phase Diagrams for Intrinsically Disordered Proteins. Biophysical journal. 2020 Jul;119(2):402–18.
Zeng, Xiangze, et al. “Connecting Coil-to-Globule Transitions to Full Phase Diagrams for Intrinsically Disordered Proteins.Biophysical Journal, vol. 119, no. 2, July 2020, pp. 402–18. Epmc, doi:10.1016/j.bpj.2020.06.014.
Zeng X, Holehouse AS, Chilkoti A, Mittag T, Pappu RV. Connecting Coil-to-Globule Transitions to Full Phase Diagrams for Intrinsically Disordered Proteins. Biophysical journal. 2020 Jul;119(2):402–418.
Journal cover image

Published In

Biophysical journal

DOI

EISSN

1542-0086

ISSN

0006-3495

Publication Date

July 2020

Volume

119

Issue

2

Start / End Page

402 / 418

Related Subject Headings

  • Thermodynamics
  • Temperature
  • Phase Transition
  • Intrinsically Disordered Proteins
  • Biophysics
  • 51 Physical sciences
  • 34 Chemical sciences
  • 31 Biological sciences
  • 06 Biological Sciences
  • 03 Chemical Sciences