Transient transformation of oligomeric structure of alpha-crystallin during its chaperone actionстатья
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Дата последнего поиска статьи во внешних источниках: 23 декабря 2016 г.
Аннотация:New evidence for dynamic behavior and flexible oligomeric structure of the molecular chaperone -
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 alpha-crystallin to fully reduced alpha-lactalbumin, used as a model protein substrate, at the stage
of its start aggregate formation results in dissociation of multimeric structure of alpha-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 alpha-crystallin dimeric form associated with destabilized monomeric
alpha-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.