AI Article Synopsis
- Protein salting-out typically creates amorphous protein gels, which are generally not useful for studying protein structure.
- Recent measurements show that these gels, made from proteins like lysozyme and IgG1, actually contain well-ordered protein nanostructures that create their hierarchical gel structure.
- These nanocrystalline domains, sized between 10-100 nm, resemble bulk crystals and could be useful for advanced structural biology techniques, enabling the study of challenging biological macromolecules.
Article 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.
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Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8561819 | PMC |
| http://dx.doi.org/10.1107/S2053230X21009961 | DOI Listing |
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