Research Scholar, Deparment of Biotechnology, IIT Guwahati. 2012-ongoing
Enzymes are ubiquitously found in nature at different milieus. It is interesting to note that homologues of enzymes exist in different environments. This leads to the belief that their stability and activity is the resultant of minute differences in their primary and secondary structures. This intrigued me to work on deciphering the differences in codon usage among thermostable, mesostable and psychrostable enzymes. Furthermore I am studying the DNA sequence of turns and loops of all the psychrophilic, mesophilic and thermophilic proteins followed by the determination of the folding kinetics, conformational folding stability, folding thermodynamics and aggregations of industrially important thermostable enzymes at different temperatures in comparison to their mesostable homologues.
Some inspiring research papers in this direction are: Lobry et al. 2006; titled “Synonymous codon usage and its potential link with optimal growth temperature in prokaryotes.” Gene. 385:128-36, and the work by Ahmad et al. 2009; titled “Thermally denatured state determines refolding in lipase: Mutational analysis.” Protein Sci. 18(6):1183-96.