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Updated: May 15, 2026

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
Published on: May 13, 2020
Transient transformation of oligomeric structure of alpha-crystallin during its chaperone action
Ekaterina Smirnova1, Natalia Chebotareva, Bella Gurvits
1Bach Institute of Biochemistry, Russian Academy of Sciences, Leninsky Prospect 33, 119071 Moscow, Russia.
Abstract:
New evidence for dynamic behavior and flexible oligomeric structure of the molecular chaperone α-crystallin is presented. Based on the results of laser dynamic light scattering, centrifugal ultrafiltration, size exclusion chromatography, analytical ultracentrifugation and electrophoresis in polyacrylamide gel, addition of α-crystallin to fully reduced α-lactalbumin, used as a model protein substrate, at the stage of its start aggregate formation results in dissociation of multimeric structure of α-crystallin. In addition to large oligomers, transient low-sized assemblies are formed with the apparent molecular mass of 50-55 kDa that corresponds to the α-crystallin dimeric form associated with destabilized monomeric α-lactalbumin. This phenomenon is suggested to represent an essential component of a transient protective mechanism tuning the stressed protein to binding sites on the exposed surface of the chaperone dimers.
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