Project titles for:
Project titles for: 2008-10
- In silico analysis of Larger subunit of AGPase in Rice and Maize
- In silico Analysis of mutated in Larger subunit of AGPase in Maize
- Structural Comparison of Betaine Aldehyde Dehydrogenase-1 of Barley and Rice
- Analysis of Gene Expression Database of Skin Cancer
- Evaluation of Sequence Alignment Tools
- Phylogenetic analysis of Drb 3.2 gene
- Modelling of Smaller subunit of AGPase in Rice and Maize
- Prediction of Protein structure from sequence
- Development of Clinical Information Database of domestic animals
- To identify distant relationship between flavoprotein superfamily
- Promoters comparison in bacteria
- Transport protein features analysis
- Genome deciphering and comparative genomics of Solanaceous genome
- Computational approach in deciphering effect of gene alteration in Arabidopsis Thaliana
- Simulation of conformational changes in protein
ADP – Glucose Phosphorylase is a key enzyme for starch synthesis in plant kingdom. It is a heterotetrameric enzyme which synthesizes the ADP-glucose, the precursor for starch synthesis. AGPase is encoded by two genes named Shrunken-2 (Sh2) and Brittle-2 (Bt2). The Sh2 gene encodes larger subunit and the Bt2 gene encodes smaller subunit. This present investigation was carried out to model the normal and specifically mutated larger subunit of AGPase enzyme in Maize. The mutation in Sh2 gene for larger subunit involved insertion of six nucleotides in Sh2 gene without changing the reading frame. This mutation resulted in to insertion of two additional amino acid residues Ser and Tyr at specific position. The direct effect of this mutation was increase in seed weight of maize up to 11-17%. To understand the factor behind this increase, we predicted the 3D structures of the normal subunit and mutated subunit by using Modeller 9v7, a comprehensive homology modelling stand alone program. The models generated were refined for energy minimization using GROMOS Force Field in Swiss-Pdb. The models generated were verified and validated with various structure refinement programs of What if Server. The models with considerably good accuracy were superimposed and compared to analyse the structural differences. From this comparison it was observed that the secondary structure content in the mutated structure had got reduced to some extent. It was due to disappearance of six residues long secondary structure segment just before the site of insertion of additional amino acid residues in mutated structure. So it seems that along with certain other factors like oligomeric interaction, dimeric interaction might play important role in increased seed weight by mutated protein in maize.