2019
DOI: 10.1038/s41467-019-10270-5
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A mechanism for reversible mesoscopic aggregation in liquid solutions

Abstract: Solutions of proteins and other molecules exhibit puzzling, mesoscopically sized inclusions of a solute-rich liquid, well outside the region of stability of the solute-rich phase. This mesoscopic size is in conflict with existing views on heterophase fluctuations. Here we systematically work out a microscopic mechanism by which a metastable solute-rich phase can readily nucleate in a liquid solution. A requisite component of the mechanism is that the solute form long-lived complexes with itself or other molecu… Show more

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Cited by 21 publications
(21 citation statements)
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“…These behaviors of wild-type p53 and p53 R248Q aggregates cohere with previous observations of mesoscopic protein-rich clusters of globular proteins (21,25,35,36). We conclude that the aggregates are mesoscopic p53-rich clusters.…”
Section: Significancesupporting
confidence: 91%
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“…These behaviors of wild-type p53 and p53 R248Q aggregates cohere with previous observations of mesoscopic protein-rich clusters of globular proteins (21,25,35,36). We conclude that the aggregates are mesoscopic p53-rich clusters.…”
Section: Significancesupporting
confidence: 91%
“…In the clusters, the transient misassembled oligomers coexist with native p53 tetramers and other stable p53 species, such as octamers, dimers, and monomers (7,39). This kinetic model accounts for the conversion of native molecules to misassembled oligomers and the diffusion of native molecules to fill the void created by this conversion as well as the outflow and decay of the transient misassembled oligomers (36,37,40). The cluster size appears as a square root of the product of the diffusivity of the misassembled oligomers and their lifetime and is, hence, independent of the protein concentration and steady in time (36,37,40).…”
Section: Significancementioning
confidence: 99%
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“…Three behaviors of the p53 R248Q aggregates cohere with previous observations of mesoscopic protein-rich clusters of both globular proteins and wild type p53. 38,43,49,50 The average cluster radius R is, first, steady and, second, independent of the protein concentration C0. The third characteristic cluster behavior exhibited by the p53 R248 aggregates is the near-exponential increase of N and φ2 with C0 (Figure 2 h,j).…”
Section: Mesoscopic Protein-rich Clusters In Solutions Of P53 R248qmentioning
confidence: 98%
“…Thirdly, the origin of the mesoscopic size of said particles is still poorly understood. There is an ongoing debate regarding the theoretical viability of the mechanism that stabilizes their size [25][26][27][28] . Even if one disregards these issues, the two-step model focuses narrowly on the initial stages of nucleation up until the formation of a crystalline cluster but makes no predictions regarding any later stages that may follow.…”
mentioning
confidence: 99%