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Nanocrystalline protein domains via salting-out.

ABSTRACT: Protein salting-out is a well established phenomenon that in many cases leads to amorphous structures and protein gels, which are usually not considered to be useful for protein structure determination. Here, microstructural measurements of several different salted-out protein dense phases are reported, including of lysozyme, ribonuclease A and an IgG1, showing that salted-out protein gels unexpectedly contain highly ordered protein nanostructures that assemble hierarchically to create the gel. The nanocrystalline domains are approximately 10-100 nm in size, are shown to have structures commensurate with those of bulk crystals and grow on time scales in the order of an hour to a day. Beyond revealing the rich, hierarchical nanoscale to mesoscale structure of protein gels, the nanocrystals that these phases contain are candidates for structural biology on next-generation X-ray free-electron lasers, which may enable the study of biological macromolecules that are difficult or impossible to crystallize in bulk.

SUBMITTER: Greene DG

PROVIDER: S-EPMC8561819 | biostudies-literature | 2021 Nov

REPOSITORIES: biostudies-literature

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Nanocrystalline protein domains via salting-out.

Greene Daniel G DG Modla Shannon S Sandler Stanley I SI Wagner Norman J NJ Lenhoff Abraham M AM

Acta crystallographica. Section F, Structural biology communications 20211019 Pt 11

Protein salting-out is a well established phenomenon that in many cases leads to amorphous structures and protein gels, which are usually not considered to be useful for protein structure determination. Here, microstructural measurements of several different salted-out protein dense phases are reported, including of lysozyme, ribonuclease A and an IgG1, showing that salted-out protein gels unexpectedly contain highly ordered protein nanostructures that assemble hierarchically to create the gel. ...[more]

PMID: 34726180

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Project description:The solubility of gases in aqueous salt solution decreases with the salt concentration, often termed the "salting-out effect." The dissolution of salt in water is followed by dissociation of salt and further solvation of ions with water molecules. The solvation weakens the affinity of gaseous molecules, and thus it releases the excess dissolved gas. Now it is interesting to know that what happens to the excess gas released during salting-out? Since it is imperative to note that the transfer of the dissolved gas in the bulk liquid may often occur in the form of nanobubbles. In this work, we have answered this question by investigating the nano-entities nucleation during the salting-out effect. The solubility of gases in aqueous salt solution decreases with the salt concentration, and it is often termed as the "salting-out effects." The dissolution of salt in water undergoes dissociation of salt and further solvation of ions with water molecules. The solvation weakens the affinity of gaseous molecules, and thus it releases the excess dissolved gas. Now it is interesting to know that what happens to the excess gas released during salting-out? While it is also imperative to note that the gas transfer in the bulk liquid often occurs in the form of bubbles. With this hypothesis, we have experimentally investigated that whether the salting-out effect nucleates nanobubble or not. What is the strong scientific evidence to prove that they are nanobubbles? Does the salting-out parameter affect the number density? The answers to such questions are essential for the fundamental understanding of the origin and driving force for nanobubble generation. We have provided three distinct proofs for the nano-entities to be the nanobubbles, namely, (1) by freezing and thawing experiments, (2) by destroying the nanobubbles under ultrasound field, and (3) we also proposed a novel method for refractive index estimation of nanobubbles to differentiate them from nano drops and nanoparticles. The refractive index (RI) of nanobubbles was estimated to be 1.012 for mono- and di-valent salts and 1.305 for trivalent salt. The value of RI closer to 1 provides strong evidence of gas-filled nanobubbles. Both positive and negative charged nanobubbles nucleate during the salting-out effect depending upon the valency of salt. The nanobubbles during the salting-out effect are stable only for up to three days. This shorter stability could plausibly be due to reduced colloidal stability at a low surface charge.

Dataset Information

Nanocrystalline protein domains via salting-out.

Publications

Nanocrystalline protein domains via salting-out.

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