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
Rice and Maize are worldwide grown crops. Both are used as staple food for human population. The grains of both crops have starch as their dry seed weight. AGPase is an enzyme which play key role in biosynthesis of Starch. AGPase catalyses the rate limiting step of ADP-glucose from Glucose- 1-phosphate and ATP. AGPase is activated in presence of 3-PGA (3-Phosphoglyceric acid) and inhibited by inorganic phosphate. AGPase is heterotetrameric in Rice and Maize, having a pair of large (LS) and a pair of small (SS) Subunit. Bt2 (Brittle 2) gene encodes for the small subunit. Bt2 subunit is catalytic subunit of AGPase. Mutation in this subunit may alter the function of AGPase and hence production of starch synthesis also affects. In this project work has been carried to model the smaller subunit of AGPase. For modelling of smaller subunit of AGPase, homology modelling method was choosen. Homology modeling was done by using Modeller9v6 program and Schrodinger program. Model built by Modeller9v6 program were best as compared to model build by Schrodinger. There are 25 % helix and 33-35% sheet in the models. The structure of smaller subunit of AGPase in rice and maize was compared and difference in secondary structure was found. This difference structure may be one of the reason for the difference in functional activity of AGPase in rice and maize.