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.

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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.

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We study protein processing ATP-dependent molecular motors that maintain protein quality control (pQC) in a cell using single-molecule force spectroscopy and enzymology. Our lab currently addresses the following three key issues pertaining to both substrate and enzyme properties key to understanding the mechanism(s) of the ATP-dependent  unfoldases and disaggregases

 

(i) mechano-chemical coupling mechanisms of the proteasomes.

(ii) disaggregation and translocation mechanisms of ATP-dependent disaggregases.

(iii) Relation between polypeptide-amino acid composition and its translocation efficiency by ATPases