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 inArabidopsis Thaliana
- Simulation of conformational changes in protein
ADP-glucose pyrophosphorylase (AGPase) (E.C. 2.7.7.27) , is an allosteric enzyme that catalyzes a rate-limiting step in starch synthesis, the conversion of glucose-1-P and ATP to ADPglucose and pyrophosphate (Hannah, 2005). Its a heterotetramer enzyme with two larger and two smaller subunits that exhibits strikingly less sequence divergence. The larger subunit encoded by Sh2 gene is the regulatory component of the enzyme and smaller one encoded by Bt2, being the catalytic. The increased seed weight of maize by 11-17% by the site specific mutagenesis of two amino acid residues, promoted the study of AGPase larger subunit of maize and rice, to find the possible reason of enhancement in maize. At the same time the failure of such an experiment on rice prompted the study of corresponding rice subunit. Though the larger subunit is not a whole sole. In this project, the task had been carried out by in silico modelling of the subunit of the two grains using Modeller9v7, a comprehensive homology modelling stand alone program. The generated models were further verified and validated and improved by various servers taking in account the energy parameters and amino acid residues propensity. The two models were superimposed and compared to analyse the structural differences. Four secondary structures were identified in maize that were found to be absent in the corresponding rice subunit. As none of these structures, were found to be a part of specific interaction sites of the subunit, the oligomeric and dimeric sites of the protein along with the way of interaction of the four subunits of the heterotetrameric protien are supposed to have an effect on the expression of the mutation in the enzyme.