Regulatory effect of A to B cattle lens alpha-crystallin subunit ratios on the quaternary structure of macromolecules formed by their assembly.
نویسندگان
چکیده
منابع مشابه
Evidence for specific subunit distribution and interactions in the quaternary structure of alpha-crystallin.
The quaternary structure of alpha-crystallin is dynamic, a property which has thwarted crystallographic efforts towards structural characterization. In this study, we have used collision-induced dissociation mass spectrometry to examine the architecture of the polydisperse assemblies of alpha-crystallin. For total alpha-crystallin isolated directly from fetal calf lens using size-based chromato...
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The mechanism of aggregation and insolubilization of lens proteins was examined based on the kinetics of crystallin-crystallin interaction determined by the surface plasmon resonance method on a BlAcore system. Lens proteins are composed mainly of three types crystallins, alpha-, beta-, and gamma-crystallin. The present study indicated that alpha-crystallin shows marked self-interaction. Furthe...
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Alpha-crystallin from the bovine eye lens was studied by small-angle neutron scattering (SANS) in 90% D2O buffer solution at 20, 50, 60, 65, 75, 85 and 95 o C. The temperature points for this study were specified on the basis of differential scanning calorimetric analysis of alpha-crystallin solutions which has shown two endothermic transitions with midpoints at 64.5 and 86 o C. The SANS study ...
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Differential scanning calorimetry was performed to monitor the heat-induced changes that occur in the structural domain of lens alpha-crystallin. Circular dichroism and fluorescence also were used to resolve the controversial issue of the quaternary structure of alpha-crystallin. Based on the thermal behavior as monitored by these techniques, a model is proposed that can account for all previou...
متن کاملThe IXI/V motif in the C-terminal extension of alpha-crystallins: alternative interactions and oligomeric assemblies.
PURPOSE Alpha-crystallin, a hetero-oligomer of alphaA- and alphaB-crystallin, is involved in maintaining eye lens transparency, primarily by its structural packing and chaperone activity. alphaA- and alphaB-crystallin share significant sequence homology, which is almost exclusively restricted to the central, conserved "alphaA-crystallin domain". The flanking N-terminal domain and C-terminal ext...
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عنوان ژورنال:
- The Journal of biological chemistry
دوره 255 4 شماره
صفحات -
تاریخ انتشار 1980