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  Salt-Dependent Rheology and Surface Tension of Protein Condensates Using Optical Traps

Jawerth, L., Ijavi, M., Ruer, M., Saha, S., Jahnel, M., Hyman, A. A., et al. (2018). Salt-Dependent Rheology and Surface Tension of Protein Condensates Using Optical Traps. Physical Review Letters, 121(25): 258101. doi:10.1103/PhysRevLett.121.258101.

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Jawerth, Louise1, Author           
Ijavi, Mahdiye2, Author
Ruer, Martine2, Author
Saha, Shambaditya2, Author
Jahnel, Marcus2, Author
Hyman, Anthony A.2, Author
Jülicher, Frank1, Author           
Fischer-Friedrich, Elisabeth1, Author           
Affiliations:
1Max Planck Institute for the Physics of Complex Systems, Max Planck Society, ou_2117288              
2external, ou_persistent22              

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 MPIPKS: Living matter
 Abstract: An increasing number of proteins with intrinsically disordered domains have been shown to phase separate in buffer to form liquidlike phases. These protein condensates serve as simple models for the investigation of the more complex membraneless organelles in cells. To understand the function of such proteins in cells, the material properties of the condensates they form are important. However, these material properties are not well understood. Here, we develop a novel method based on optical traps to study the frequency-dependent rheology and the surface tension of P-granule protein PGL-3 condensates as a function of salt concentration. We find that PGL-3 droplets are predominantly viscous but also exhibit elastic properties. As the salt concentration is reduced, their elastic modulus, viscosity, and surface tension increase. Our findings show that salt concentration has a strong influence on the rheology and dynamics of protein condensates suggesting an important role of electrostatic interactions for their material properties.

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 Dates: 2018-12-182018-12-21
 Publication Status: Issued
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Title: Physical Review Letters
  Abbreviation : Phys. Rev. Lett.
Source Genre: Journal
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Publ. Info: Woodbury, N.Y. : American Physical Society
Pages: - Volume / Issue: 121 (25) Sequence Number: 258101 Start / End Page: - Identifier: ISSN: 0031-9007
CoNE: https://pure.mpg.de/cone/journals/resource/954925433406_1