IISER MOHALI

Professor , Biological Sciences

Email

guptasarma(AT)iisermohali.ac.in

Phone

+91 172 2293151

Fax

+91 172 2240266

Personal Page

 www.guptasarmalab.in

Research Area

Protein Engineering & Structural Biochemistry

INTERESTS: My main interests lie in understanding and engineering the manner in which globular proteins fold; in why (and how) they misfold; in what these misfolded forms do (to cause human disease) or can be made to do (e.g., conduct electricity); in what determines the thermodynamic and kinetic stabilities of the folded, native forms of globular proteins (especially those evolved to function in extremophile microbes); and in developing approaches through which the activities and functions of globular proteins and enzymes can be altered through rational and/or combinatorial mutagenesis.

APPROACHES: I commonly employ (and also occasionally develop) preparative and analytical methods/approaches deriving from different forms of electronic and vibrational spectroscopy, mass spectrometry, biomolecular chromatography, electrophoresis, computation, calorimetry, microscopy, and recombinant DNA-based experimentation, and also certain other tools/techniques of organic and physical biochemistry.

ET CETERA: In addition, I also love to dwell upon (and occasionally contribute to) current understanding of the mechanistic basis of regulation of gene expression, and the cellular and molecular basis of development.

Selected Publications

• Sharma P, Kaila P, Guptasarma P. (2016). Creation of active TIM barrel enzymes through genetic fusion of half-barrel domain constructs derived from two distantly related glycosyl hydrolases. FEBS Journal 283, 4340-4356.

• Khan JM, Sharma P, Arora K, Kishor N, Kaila P, Guptasarma P. (2016). The Achilles' Heel of "Ultrastable" Hyperthermophile Proteins: Submillimolar Concentrations of SDS Stimulate Rapid Conformational Change, Aggregation, and Amyloid Formation in Proteins Carrying Overall Positive Charge. Biochemistry 55, 3920-3936.

• Sharma P, Guptasarma P. (2017). Endoglucanase activity at a second site in Pyrococcus furiosus triosephosphate isomerase-Promiscuity or compensation for a metabolic handicap? FEBS Open Bio 7, 1126-1143.

• Arora K, Thakur B, Mrigwani A, Guptasarma P. (2021). N-Terminal Extensions Appear to Frustrate HU Heterodimer Formation by Strengthening Intersubunit Contacts and Blocking the Formation of a Heterotetrameric Intermediate. Biochemistry 60, 1836-1852.

• Thakur B, Arora K, Gupta A, Guptasarma P. (2021). The DNA-binding protein HU is a molecular glue that attaches bacteria to extracellular DNA in biofilms. Journal of Biological Chemistry 296, 100532.