Research Activities in 2012
In the genetic code ,the 61 codons encode the 20 amino acids whic results more than one codon for most of the amino acids ,known as synonymous codons. The abundance of these synonymous codons in genomes is not random suggesting the role of evolutionary forces driving the bias in genomes.Interestingly, the extent of codon usage bias is different among different species and different within a genome. Therefore to understand the evolutionary mechanism of this wide spread phenomenon is of significant interest to evolutionary scientists. We are addressing the problem by doing compositional analysis of nucleotides at 4-fold degenerate sites across eight family boxes. Our observation is in the support that selection is important to cause codon usage bias in genomes
Isoniazid is a first line tuberculosis drug used to treat tuberculosis. This prodrug is activated by Mycobacterial catalase -peroxidase and Ser315Thr mutation is found to affect the activation process. Docking studies were performed in order to find the effect of mutation on Isoniazid binding to the active site. The change in the Isoniazid binding pattern is mainly responsible for the Isoniazid resistance Mycobacterium tuberculosis. In order to find alternative to Isoniazid certain imidazole derivatives are chosen for docking analysis and among them 4-nitro-1H-imidazole-5-carbohydrazide shows very good result
It has been established that the Intrinsically Disordered Proteins (IDPs) are functionally as important as the other proteins without having a completely folded conformation under the native, physiological conditions. These unstructures/disordered regions provide advantages in several protein functions. The IDPs of class four with known crystallographic structure have been selected for analysis. The PI values of these proteins are very selective and in the range of 3.5-4.0, which is different from the globular proteins. The amino acid composition of the disordered region sequences has been calculated to find the specificity of these segments and their functional importance.
The percentage composition of amino acids of the disordered regions of IDPs has ben compared with the percentage occurrence of amino acids in the completely folded (globular) proteins and the result show a qualitative difference from the available data in the literature. The investigation done in this project gives a strong indication that the intrinsically disordered proteins are divergent and a comprehensive research is very much required to understand the specificity of these proteins and also to explore the mechanism of the functions done by IDPs.