• Ashutosh Mukherjee
• Asis Kumar Pal

In this study, a glutamate decarboxylase (GAD) protein from Selaginella moellendorffii was analyzed in silico to predict its physicochemical properties and three-dimensional structure. The computed heoretical isoelectric point (pI) was found to be less than 7 indicating the acidic nature of this protein. The aliphatic index of 91.64 indicates the thermal stability of the protein. Grand average hydropathy (GRAVY) was predicted to be -0.224 which shows the possibility of better interaction of this protein with water. Secondary structure analysis revealed the predominance of alpha helix followed by random coil, extended strand and beta turns. It is also predicted that the protein is localized on the endoplasmic reticulum membrane. Homology modeling revealed the three-dimensional structure of the protein which shows that the protein contains 19 alpha helices, 3 beta sheets with 13 strands and 3 beta alpha beta units. This study will benefit further laboratory based evaluation of this protein and will also benefit evolutionary study of GAD proteins as a whole.

"Computational analysis of a Glutamate decarboxylase (GAD) protein from Selaginella moellendorffii", International Journal of Emerging Technologies and Innovative Research (www.jetir.org), ISSN:2349-5162, Vol.8, Issue 12, page no.d348-d353, December-2021, Available :http://www.jetir.org/papers/JETIR2112343.pdf

"Computational analysis of a Glutamate decarboxylase (GAD) protein from Selaginella moellendorffii", International Journal of Emerging Technologies and Innovative Research (www.jetir.org | UGC and issn Approved), ISSN:2349-5162, Vol.8, Issue 12, page no. ppd348-d353, December-2021, Available at : http://www.jetir.org/papers/JETIR2112343.pdf