Investigation of Folding of Purified Recombinant GRA1 Protein Using Web Based Protein Disorder Servers and Trypsin Digestion

Author(s): Mert Doskaya, Ayse Caner, Aysu Degirmenci, Frances Jurnak, Yuksel Guruz.

Journal Name: Protein & Peptide Letters

Volume 16 , Issue 7 , 2009

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The successful folding of a recombinant protein after expression and purification is essential for structural, biochemical and vaccination studies. Toxoplasma gondii recombinant GRA1 protein is a promising vaccine candidate against toxoplasmosis. In the present study, the folding of recombinant GRA1 protein has been evaluated by web based bioinformatics tools that predict protein folding. Subsequently, trypsin digestion, which is a simple indication of proper protein folding, has been used to determine whether recombinant GRA1 protein is likely to be folded. The results indicate that the recombinant GRA1 protein is predicted to be folded by most of the web based bioinformatics predictors. Moreover, in protease digestion experiments, the recombinant GRA1, which was purified to homogeneity without the use of denaturants, gives rise to a discrete band pattern that is indicative of a folded protein. Together, the results suggest that recombinant GRA1 protein is in a folded conformation, suitable for structural, biochemical and vaccination studies.

Keywords: Toxoplasma gondii, dense granules, recombinant GRA1 protein, trypsin digestion, web based bioinformatics tools

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Article Details

Year: 2009
Page: [834 - 841]
Pages: 8
DOI: 10.2174/092986609788681832
Price: $65

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