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Stabilization of CrystallinsThe water-soluble structural protein so called crystallin is important components of lens andcornea of the eye. It contributes for the transparency of the eye and its alterations can lead toadverse events on the appearance and visionCrystallin is a soluble protein of vertebrate eye lens (Wistow & Slingsby, 2010). The neatcomplement of crystalline is sensitive to evolutionary pressures and adaptation in differentvertebrate lineages. There are three classes of crystallins including α, β and γ-crystallins.Crystallin stability appears to be influenced by chemical denaturants, pH, and specificmutations (Serebryany et al., 2014). However the extent of stability differs with the class ofcrystalline. Kosinski-Collins and King (2003) investigated the effect of chemical treatment onfolding of γD crystallins and found that the crystllins possess significant hysteresis. (Sahin etal (2011) revealed that the destabilization of the C-terminal domain diminishes the hysteresis.From the available sources, it can be understood that no or little information is available forthe stabilization of γD crystallins. The objective of the paper is to describe the experimental procedure for the stabilization ofγD crystallins. The crystalline solution (50-100 mM) will be prepared in phosphate buffersaline pH 7.4. Various solutions comprising of polymers (E.g., PVP) or polyhydric alcohol(PEG 400, mannitol etc) will be prepared. Known amount (0 serves for control, 5-100% v/v)of solution will be added to the crystalline solution. All the solutions will be subjected for theexposure to radiation with UV light under standard conditions. The three dimensional imagesutilizing X-ray crystallography will be taken to estimate the type and concentration ofstabilizer. ReferencesKosinski-Collins, M.S & King, J (2003) In vitro unfolding, refolding, and polymerization ofhuman gammaD crystallin, a protein involved in cataract formation. Protein Sci.12(3), 480-90Serebryany, E., & King, J. A. (2014). The βγ-crystallins: Native state stability and pathwaysto aggregation.Progress in Biophysics and Molecular Biology,115(1), 32–41. Wistow, G & Slingsby, C (2010) Structure and evolution of crystallins. The Encyclopedia ofthe Eye. 2, 229–2381
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