2022
DOI: 10.1101/2022.11.21.517354
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The Effect of Polymer Length in Phase Separation

Abstract: Understanding the thermodynamics that drives liquid-liquid phase separation (LLPS) is quite important given the many numbers of diverse biomolecular systems undergoing this phenomenon. Regardless of the diversity, the processes underlying the formation of condensates exhibit physical similarities. Many studies have focused on condensates of long polymers, but very few systems of short polymer condensates have been observed and yet studied. Here we study a short polymer system of various lengths of poly-Adenine… Show more

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(4 citation statements)
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“…38 Apart from through maturation or aging (the time-dependent coarsening and loss of dynamicity) of a liquidlike droplet by RNA binding proteins such as FUS, pathogenic fibrils can also be formed by proteins such as Aβ directly through irreversible aggregation without LLPS, which is termed liquid-solid phase separation (LSPS). 39 In addition to full-length proteins and their LC domains, short peptides are able to phase separate, forming liquid condensates [40][41][42][43] and reversible or irreversible fibrils. 12,13,15 Recent crystal structure studies of short peptides have provided different structural properties of the two types of fibrils.…”
Section: Introductionmentioning
confidence: 99%
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“…38 Apart from through maturation or aging (the time-dependent coarsening and loss of dynamicity) of a liquidlike droplet by RNA binding proteins such as FUS, pathogenic fibrils can also be formed by proteins such as Aβ directly through irreversible aggregation without LLPS, which is termed liquid-solid phase separation (LSPS). 39 In addition to full-length proteins and their LC domains, short peptides are able to phase separate, forming liquid condensates [40][41][42][43] and reversible or irreversible fibrils. 12,13,15 Recent crystal structure studies of short peptides have provided different structural properties of the two types of fibrils.…”
Section: Introductionmentioning
confidence: 99%
“…39 Unlike the irreversible fibrils, the structures of reversible fibrils are organized in kinked strands perpendicular to the fibril spine, or extended β-strands with a hydrous sheet interface, or a stacking pattern with Asp residues from individual β-strands aligned along the fibril spine. 7,12,13,16 For example, fibrils of FUS [37][38][39][40][41][42] (PDB ID: 5XSG) comprise kinked strands without extended β sheets (Fig. S1A †), and fibrils of FUS [54][55][56][57][58][59] (PDB ID: 5XRR) consist of pairs of β-sheets with a hydrophilic interface (Fig.…”
Section: Introductionmentioning
confidence: 99%
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