Investigation of Folding of Purified Recombinant GRA1 Protein Using Web Based Protein Disorder Servers and Trypsin Digestion
Küçük Resim Yok
Tarih
2009
Dergi Başlığı
Dergi ISSN
Cilt Başlığı
Yayıncı
Bentham Science Publ Ltd
Erişim Hakkı
info:eu-repo/semantics/closedAccess
Özet
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.
Açıklama
Anahtar Kelimeler
Toxoplasma gondii, dense granules, recombinant GRA1 protein, trypsin digestion, web based bioinformatics tools, protein folding
Kaynak
Protein and Peptide Letters
WoS Q Değeri
Q3
Scopus Q Değeri
Cilt
16
Sayı
7
