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
Arabidopsis thaliana is a small plant from the mustard family that has become the model system of choice for research in plant biology. The 120-megabase genome of Arabidopsis was organized into 5 chromosomes and contains an estimated 20,000 genes. Crys are members of a larger blue light-absorbing chromo protein superfamily that also includes the DNA photolyase. Functional characterization of cry2 was mainly involved in the control of flowering and of hypocotyls elongation. A single base alteration or a site directed mutagenesis in cry2 gene confers early flowering under short-day conditions in one tropical accession of Arabidopsis. In this project, the work has been carried out to model 3D structures of cry2 normal gene and cry2 altered gene proteins using homology modelling High similarity score but crucial structural differences play important role in protein function. Cry2 normal and Cry2 altered proteins show a high percentage similarity but structural dissimilarity. Hence, this structural dissimilarity responsible for the early flowering and inhibition in hypocotyle elongation in Arabidopsis plant. In the current investigation two domains were found for each normal and altered.cry2 proteins A site directed mutagenesis in one domain (PHR) at 367 position may have altered the protein function, Deazaflavin (a light-harvesting molecule) chromophore is responsible for activity of the protein and bind specifically to the protein active site. Binding sites on the crystallographic structure of cry2 normal and cry2 altered were examined with the structure based design program DOCK 6.1. The ligands were screened for their ability to dock within the catalytic traid of protein. Low energy conformation of the altered gene as compare to the normal gene showed that the ligand molecule best fit or docked with the protein and unique conformation generated for ligand varied enormously, and gave some perception of the flexibility. The total energy of receptor-ligand complexes in best fit mode has also been calculated. The scoring grid was generated with normal cry2 or altered cry2, 3,595,394 and 5,252,800 grid points. The final dock output showed the docking of the ligand.