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Significance One common feature conserved across living systems is the presence of a high concentration of crystallin proteins packed within the eye lens. The polydispersity of crystallins in the vertebrate… Click to show full abstract
Significance One common feature conserved across living systems is the presence of a high concentration of crystallin proteins packed within the eye lens. The polydispersity of crystallins in the vertebrate lens is one factor that may prevent crystallization from the dense protein array within lens fiber cells. We probe the spatial distribution and assembly mechanics of the β-subtype in bovine lens. We assay hydrodynamic behavior in different salts and observe altered protein polydispersity in vitro. Our results describe reversible changes in size and surface charge of β-oligomers that are regulated by divalent cations. Our data suggest a dynamic equilibrium that produces the inherent polydispersity of β-crystallin as an important feature of lens function and stability.
Journal Title: Proceedings of the National Academy of Sciences of the United States of America
Year Published: 2022
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