Prof. Rajiv Bhat
 

Dr. Rajiv Bhat
Professor
Ph:  +91 11 26704086
Email: rajivbhat@mail.jnu.ac.in
                       
Education: 

Ph.D. (Biophysical Chemistry), IIT, New Delhi.
M.Sc. (Physical Chemistry), University of Jammu, Jammu.

Career:

2004 -
Professor, School of Biotechnology, JNU, New Delhi.
1998-2004
Associate Professor, Special Centre for Biotechnology, JNU, New Delhi.
2000-2001
Visiting Scientist, Department of Chemistry and Chemical Biology, Cornell University, Ithaca, NY, USA.
1990-1998
Assistant Professor, Special Centre for Biotechnology, JNU, New Delhi.
1989-1990
Lecturer, Deptt. of Biochemistry, University of Delhi, New Delhi.
1986-1989
Postdoctoral Associate, Graduate Deptt. of Biochemistry, Brandeis University,  Waltham, Massachusetts, USA.
1985-1986
Lecturer in Chemistry, Thapar Institute of Engineering and Technology, Patiala.

Area of Interest:

  • Protein Stability and Folding: Thermodynamic and Kinetic aspects
  • Bimolecular Structure and Interactions: Microcalorimetry and Spectroscopy.

Summary of research:

We are interested in the role of solvent environment in the stability and folding of proteins for which we use a combination of thermodynamic and spectroscopic tools. We employ Differential Scanning Calorimetry and Isothermal Titration Calorimetry to probe protein stability and protein-ligand interactions and spectroscopic tools like UV-Visible, fluorescence, Circular dichroism, and Infrared for structural characterization. We are currently using hexokinase A and glucose oxidase for stability studies and citrate synthase, carbonic anhydrase, recombinant human γD-crystallin and synucleins for folding and aggregation studies as models.

Honors/Awards:

  • Merit Certificate for I rank in College/University in Pre-University Course, B.Sc., and M.Sc.
  • National Merit Scholarship for postgraduate studies
  • Biotechnology Overseas Associateship Award, Department of Biotechnology, Govt. of India, 2000-2001

Selected Publications:

  1. R. Mishra, R. Bhat, and R. Seckler (2007). Chemical chaperone mediated protein folding: Stabilization of P22 tailspike folding intermediates by glycerol. Biol. Chem., 388: 797-804.
  2. A. Tiwari and R. Bhat (2006). Stabilization of yeast hexokinase A by polyol osmolytes: Correlation with the physicochemical properties of aqueous solutions, Biophys. Chem., 124: 90-99.
  3. R. Mishra, R. Seckler, and R. Bhat (2005). Efficient refolding of aggregation prone citrate synthase by polyol osmolytes: How well are folding and stability aspects coupled? J. Biol. Chem., 280: 15553-15560.
  4. A. E. Welker, K. Maki, M. C. R. Shastry, D. Juminaga, R. Bhat, H. A. Scheraga, and H. Roder (2004).Ultra–rapid mixing experiments shed new light on the characteristics of the initial conformational ensemble during the folding of Ribonuclease, Proc. Natl. Acad. Sci. USA, 101: 17681-17686.
  5. D. Prasanna Kumar, A. Tiwari and R. Bhat (2004). Effect of pH on the stability and structure of yeast hexokinase A: Acidic amino acid residues in the cleft region are critical for the opening and the closing of the structure. J. Biol. Chem., 279: 32093-32099.
  6. J. K. Kaushik and R. Bhat (2003).Why is trehalose an exceptional protein stabilzer?: An analysis of the thermal stability of proteins in the presence of the compatible osmolyte trehalose. J. Biol. Chem., 278: 26458-26475.
  7. R. Bhat, W. J. Wedemeyer, and H. A. Scheraga (2003). Proline isomerization in bovine pancreatic ribonuclease A. 2. Folding conditions, Biochemistry, 42: 5722-5728.
  8. A. Tiwari, D. Prasanna Kumar, and R. Bhat (2000). An efficient and cost-effective procedure for preparing samples for Differential Scanning Calorimetry Experiments, Anal. Biochem., 284: 406-408.
  9. J.K. Kaushik and R. Bhat (1999). A mechanistic analysis of the increase in the thermal stability of proteins in aqueous carboxylic acid salt solutions, Protein Sci., 8: 222-233.
  10. J.K. Kaushik and R. Bhat (1998). Thermal stability of proteins in aqueous polyol solutions: Role of the surface tension of water in the stabilizing effect of polyols, J. Phys. Chem. B, 102: 7058-7066.

 

 

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