In the current era of interdisciplinary research, it is both important and stimulating to work at the interface of biochemistry/physical chemistry and biophysics. Our lab probes the mechano-chemical features of biological macro molecules, proteins and enzymes. We employ single-molecule force spectroscopy tools such as SM-AFM in addition to the other biochemical, spectroscopic and biophysical tools to probe these systems. Current lab interests are briefly described below

Knotted proteins: Knotted proteins are a special class of proteins in which the backbone crossesover itself forming knots, challenging our understanding of protein folding. In addition to the folding mechanisms, the functional significance of these knots in naturally occuring proteins has not been understood well. In our lab, we try to untangle the folding/unfolding, degradation and physiological relavance of these knotted proteins using a variety of spectroscopic, biophysical and biochemical methods.












Proteasomes, machines of protein degradation: Protein degradation is a key cellular process that maintains healthy proteome in the cell and prevents may diseases. This protein destruction is carried out in a directed manner by proteasomes and proteases. Both these enzymes act as molecular motors and convert chemical energy to mechanical energy to perform this function. In our lab we study the mechanism of action of these enzymes i.e, proteases and proteasomes from various organisms, In particular, we work on proteasome from Mycobacterium Tuberculosis to determine its mechanism of action, oligomerization and compare degradation power among various proteases and proteasomes









Mechanical stability of proteins involved in cell division: Many protein assemblies are responsible for cell division in bacteria, of which FtsZ is a key player. It is also an importanct target protein for drug discovery on antibiotics. Our lab is involved in understanding the mechanical properties of this FtsZ protein which plays a key role during cell division.










Single molecule force spectroscopy tools such as optical tweezers and Single-molecule AFM have enhanced our understanding of the mechanical properties of proteins as well as motor mechanisms of numerous molecular motors. For example, providing details about the forces that proteins can resist, mechanical unfolding pathways of proteins, how molecular motors move on their “tracks”, and the energetic costs of these processes among others These techniques complement the solution biochemical/biophysical methods by allowing for the examination of individual processes of the multi-step reactions and highlight the heterogeneity in the molecular properties.