A scale-invariant log-normal droplet size distribution below the critical concentration for protein phase separation

Tommaso Amico; Samuel Dada; Andrea Lazzari; Michaela  Brezinova; Antonio Trovato; Michele Vendruscolo; Monika Fuxreiter; Amos Maritan

doi:10.7554/eLife.94214.3

A scale-invariant log-normal droplet size distribution below the critical concentration for protein phase separation

Tommaso Amico, Samuel Dada, Andrea Lazzari, Michaela Brezinova, Antonio Trovato, Michele Vendruscolo, Monika Fuxreiter, Amos Maritan

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review

Abstract

Many proteins have been recently shown to undergo a process of phase separation that leads to the formation of biomolecular condensates. Intriguingly, it has been observed that some of these proteins form dense droplets of sizeable dimensions already below the critical concentration, which is the concentration at which phase separation occurs. To understand this phenomenon, which is not readily compatible with classical nucleation theory, we investigated the properties of the droplet size distributions as a function of protein concentration. We found that these distributions can be described by a scale-invariant log-normal function with an average that increases progressively as the concentration approaches the critical concentration from below. The results of this scaling analysis suggest the existence of a universal behaviour independent of the sequences and structures of the proteins undergoing phase separation. While we refrain from proposing a theoretical model here, we suggest that any model of protein phase separation should predict the scaling exponents that we reported here from the fitting of experimental measurements of droplet size distributions. Furthermore, based on these observations, we show that it is possible to use the scale invariance to estimate the critical concentration for protein phase separation.

Original language	English
Article number	RP94214
Journal	eLife
Volume	13
Number of pages	16
ISSN	2050-084X
DOIs	https://doi.org/10.7554/eLife.94214.3
Publication status	Published - 18 Nov 2024
Externally published	Yes

Keywords

critical exponents
none
phase transitions
physics of living systems
protein condensation
universal behaviour

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10.7554/eLife.94214.3Licence: CC BY

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title = "A scale-invariant log-normal droplet size distribution below the critical concentration for protein phase separation",

abstract = "Many proteins have been recently shown to undergo a process of phase separation that leads to the formation of biomolecular condensates. Intriguingly, it has been observed that some of these proteins form dense droplets of sizeable dimensions already below the critical concentration, which is the concentration at which phase separation occurs. To understand this phenomenon, which is not readily compatible with classical nucleation theory, we investigated the properties of the droplet size distributions as a function of protein concentration. We found that these distributions can be described by a scale-invariant log-normal function with an average that increases progressively as the concentration approaches the critical concentration from below. The results of this scaling analysis suggest the existence of a universal behaviour independent of the sequences and structures of the proteins undergoing phase separation. While we refrain from proposing a theoretical model here, we suggest that any model of protein phase separation should predict the scaling exponents that we reported here from the fitting of experimental measurements of droplet size distributions. Furthermore, based on these observations, we show that it is possible to use the scale invariance to estimate the critical concentration for protein phase separation.",

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author = "Tommaso Amico and Samuel Dada and Andrea Lazzari and Michaela Brezinova and Antonio Trovato and Michele Vendruscolo and Monika Fuxreiter and Amos Maritan",

year = "2024",

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AU - Amico, Tommaso

AU - Dada, Samuel

AU - Lazzari, Andrea

AU - Brezinova, Michaela

AU - Trovato, Antonio

AU - Vendruscolo, Michele

AU - Fuxreiter, Monika

AU - Maritan, Amos

PY - 2024/11/18

Y1 - 2024/11/18

N2 - Many proteins have been recently shown to undergo a process of phase separation that leads to the formation of biomolecular condensates. Intriguingly, it has been observed that some of these proteins form dense droplets of sizeable dimensions already below the critical concentration, which is the concentration at which phase separation occurs. To understand this phenomenon, which is not readily compatible with classical nucleation theory, we investigated the properties of the droplet size distributions as a function of protein concentration. We found that these distributions can be described by a scale-invariant log-normal function with an average that increases progressively as the concentration approaches the critical concentration from below. The results of this scaling analysis suggest the existence of a universal behaviour independent of the sequences and structures of the proteins undergoing phase separation. While we refrain from proposing a theoretical model here, we suggest that any model of protein phase separation should predict the scaling exponents that we reported here from the fitting of experimental measurements of droplet size distributions. Furthermore, based on these observations, we show that it is possible to use the scale invariance to estimate the critical concentration for protein phase separation.

AB - Many proteins have been recently shown to undergo a process of phase separation that leads to the formation of biomolecular condensates. Intriguingly, it has been observed that some of these proteins form dense droplets of sizeable dimensions already below the critical concentration, which is the concentration at which phase separation occurs. To understand this phenomenon, which is not readily compatible with classical nucleation theory, we investigated the properties of the droplet size distributions as a function of protein concentration. We found that these distributions can be described by a scale-invariant log-normal function with an average that increases progressively as the concentration approaches the critical concentration from below. The results of this scaling analysis suggest the existence of a universal behaviour independent of the sequences and structures of the proteins undergoing phase separation. While we refrain from proposing a theoretical model here, we suggest that any model of protein phase separation should predict the scaling exponents that we reported here from the fitting of experimental measurements of droplet size distributions. Furthermore, based on these observations, we show that it is possible to use the scale invariance to estimate the critical concentration for protein phase separation.

KW - critical exponents

KW - none

KW - phase transitions

KW - physics of living systems

KW - protein condensation

KW - universal behaviour

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DO - 10.7554/eLife.94214.3

M3 - Journal article

SN - 2050-084X

VL - 13

JO - eLife

JF - eLife

M1 - RP94214

ER -

A scale-invariant log-normal droplet size distribution below the critical concentration for protein phase separation

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Keywords

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