Structural Studies of E.coli thioredoxin and Plasmodium falciparum Triosephosphate Isomerase using NMR and Computational Methods

To unravel the mysteries of complex biological processes carried out by biomolecules it is necessary to adopt a multifaceted approach, which involves employing a wide variety of tools both computational and experimental. In order to gain a clear understanding of the function of biomolecules their three dimensional structure is required. This study is concerned with the structure, mode of interaction and dynamic properties of a redox active protein, viz., thioredoxin, an enzyme triosephosphate isomerase, the effect on activity of this enzyme by the regulator glutathione and the control of this regulation by the thioredoxin. The preferential role of reduced thioredoxin in effecting such redox regulation as well as in the more general non-redox regulation of proteins in the cell is explored in terms of the role of dynamics in protein recognition by thioredoxin. The influence of allosteric disulfide on the structure and dynamics of thioredoxin has been explored. Several methods have been invoked to study these properties ranging from biochemical assays, nuclear magnetic resonance, mass spectrometry and computational methods.