Prof. Rajiv Bhat
 

Dr. Rajiv Bhat
Professor
Tel: +91 11 26704086
Fax: +91 11 26738747
Email: rajivbhat@mail.jnu.ac.in; rajivbhat@hotmail.com
Web Links : https://scholar.google.co.in/citations?user=cPs03xMAAAAJ&hl=en          
                    http://academictree.org/chemistry/peopleinfo.php?pid=66726

Education: 

Ph.D. (Biophysical Chemistry), IIT, Delhi (1986)

M.Sc. (Physical Chemistry), University of Jammu (1980)

B.Sc. (Biology and Chemistry), University of Jammu (1978)

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.
2009-2011
Dean, School of Biotechnology, Jawaharlal Nehru University, New Delhi

2011-2013

2012-17

Director of Admissions, Jawaharlal Nehru University, New Delhi

Programme Coordinator, Inter-School project in the area of “Chemical and Synthetic Biology” (DBT-BUILDER) involving five Science Schools of JNU
2011-2015
Secretary, Indian Biophysical Society


Areas of Interest:

  • Aggregation and Amyloid formation in neurodegenerative and other diseases. Discovery of natural products as potential inhibitors and modulators of aggregation-related diseases. Intrinsically disordered proteins and protein homeostasis
  • Bimolecular Structure and Interactions: Role of water and weak interactions
  • Use of Chemical Chaperones in controlling protein misfolding and amyloid formation
  • Structural and functional stabilization of proteins and enzymes by stress-osmolytes and technology development for stabilizing therapeutic proteins

Summary of research:

Protein misfolding, aggregation and amyloid formation is involved in a number of neurodegenerative, metabolic and oncogenic diseases. We are interested in exploring the proteins involved in these diseases and in probing the role of chemical chaperones and natural products in the inhibition and modulation of their aggregation and understanding their mechanism of action. The studies involve expression, purification, and site-directed mutagenesis of these proteins using the tools of molecular biology, protein chemistry, structural biology, mammalian cell culture, toxicity studies, confocal microscopy and live cell imaging. Structural Biology tools include UV-Visible, CD, fluorescence, and IR spectroscopy. In addition, Transmission Electron Microscopy and Dynamic Light Scattering is employed for visualizing structures and aggregate sizes. Biomolecular interactions and stability studies are carried out using Isothermal Titration Calorimetry and Differential Scanning Calorimetry. Currently we are using Recombinant human brain Synucleins (α, β, and γ) and their familial disease causing mutants as systems of Parkinson’s disease and recombinant human lysozyme and its mutants involved in amyloidoses. Another protein of interest is transthyretin involved in peripheral neuropathy.

We are also interested in understanding the role of water and weak interactions, and that of chemical chaperones and osmolytes on the stability, folding, misfolding and aggregation of a number of model proteins. Insights gained from these studies are being applied for structurally and functionally stabilizing therapeutically important proteins like human insulin, industrially important enzymes and some cytokines.

Honors/Awards/Fellowship:

• Merit Certificate for I rank in College/University in Pre-University Course

• Merit Certificate for I rank in College B.Sc.

• Merit Certificate for I rank in M.Sc. Chemistry

• National Merit Scholarship for postgraduate studies

• Awarded Junior and Senior research fellowships of IIT, Delhi.

• Postdoctoral Research Fellowship of National Institutes of Health (USA).

• Young Investigator Travel Award of 'The Protein Society' to participate in their Second Symposium in San Diego, USA, 1988.

• Biotechnology Overseas Associateship Award, Department of Biotechnology, Govt. of India, 2000-2001.

Membership of Learned Societies

American Chemical Society, 1984-1990

IUPAC, 1986-1990; American Inst. of Chemists, 1987-1989

Protein Society, 1987-1990, 2004; Society of Biological Chemists (India)-life member

Indian Biophysical Society-Life member

Research activities

Ph.D. student theses completed: 12

  1. Solvent mediated thermal stability of proteins, J.K.Kaushik (1997).

  2. Cosolvent assisted protein refolding: Chymotrypsinogen as a model, G.M.Vani     (1997).

  3. Differential scanning calorimetric studies on the thermal stabilization of yeast                   hexokinase A by solvent additives, Ashutosh Tiwari (1999).

  4. Cosolvent assisted folding of proteins: Studies on citrate synthase and P22 tailspike protein, Rajesh Mishra (2002).

  5. Solvent mediated thermal stability and refolding of yeast hexokinase A, D. Prasanna Kumar (2003).

  6. Studies on thermostabilization of protective antigen of B. anthracis, Samer Singh (joint with Prof. R. Bhatnagar) (2003).

  7. Effect of osmolytes of the polyol and amino acid series on the stability of glucose oxidase, Neeraj K. Mishra (2007).

  8. Effect of solvent environment on stability, folding and aggregation of human γDcrystallin, Saurabh Singh (2009).

  9. Studies on the refolding of bovine carbonic anhydrase (BCA II) in the presence of cosolvent additives, Swapnil Gupta (2010).

  10. Expression, purification and characterization of human recombinant α, β, and γ synuclein proteins involved in neurodegeneration, Manish K. Jain (2012).

  11. Understanding the mechanism of the effect of polyols and polyphenols on the stability and amyloid fibril formation of recombinant human lysozyme, Fatima K. Zaidi (2016).

  12. Studies on the Effect of Various Polyphenols and Polyols on Structure and Aggregation of Recombinant Human γ-Synuclein, Sneha Roy (2018, submitted).


    Ph.D. students (on-going): 2

    M. Sc. research projects completed: 50

Courses Taught

  1. Biophysical Chemistry - 3 credits (M.Sc.)
  2. Laboratory Techniques -2 credits (M.Sc.)
  3. Advances in Protein Chemistry-2 credits (M.Sc.)
  4. Advance Discussion course on Protein Stability and Folding -3 credits (Pre-Ph.D.)

Reviewer of  Journals

Have reviewed for Scientific Reports, Biophysical Journal, Biochemistry, Biophysical Chemistry, Journal of Physical Chemistry B, Protein Science, Proteins: Structure, Function and Bioinformatics, Journal of Chemical Thermodynamics, Biotechnology and Bioengineering, Applied Biochemistry and Biotechnology, International Journal of Pharmaceutics, Indian Journal of Biochemistry and Biophysics, Journal of Scientific and Industrial Research, Indian Journal of Biotechnology.

Reviewer of Ph.D. theses

Reviewed Ph.D. theses from University of Delhi, IIT Delhi, IIT Bombay, National Centre for Biological Sciences (NCBS), IISER, Mohali, Jamia Millia Islamia, Banaras Hindu University, Ambedkar Centre for Biomedical Research, University of Hyderabad, University of Pune, Guru Nanak Dev University, Panjab University, University of Jammu, Central Food Technology Research Institute, Osmania University, National Dairy Research Institute

Reviewer of Grants

Have reviewed grant proposals from Department of Science and Technology, Department of Biotechnology, Council of Scientific and Industrial Research, and from Israel Science Foundation.

Sponsored Projects

  1. Effect of solvents on the thermal stability of proteins, Department of Science and Technology, Duration: 1993-96.
  2. Protein engineering of protective antigen from Bacillus anthracis: Computational and genetic engineering approach, Department of Biotechnology (joint with Prof. R. Bhatnagar), Duration: 1999-2002.
  3. Enhancing folding and stability of glucose oxidase by solvent engineering, Council of Scientific and Industrial Research, Duration: 2001-2004.
  4. Thermostabilization of recombinant Protective Antigen of Bacillus anthracis by solvent additives, NATP/World Bank (joint with Prof. R. Bhatnagar), Duration: 2002-2005.
  5. Folding, stability, energetics, and biomolecular interactions in proteins, UGC (UPOE-1) Duration: 2002-2007.
  6. High precision microcalorimetric facility for monitoring biomolecular stability and interactions, DBT, Duration: 2006-2010.
  7. From molecules to systems: Exploring biological space using chemical and synthetic biology, Department of Biotechnology, Govt. of India, (DBT-BUILDER) 2012-2019.

Publications:

  1. Effect of polyols on the structure and aggregation of recombinant human γ-Synuclein, an intrinsically disordered protein,S. Roy and R. Bhat,Biochim. Biophys. Acta, Proteins Proteomics, (doi.org/10.1016/j.bbapap.2018.07.003) (2018).
  2. Comparative analysis of the conformation, aggregation, interaction, and fibril
    morphologies of human α, β, and γ synuclein proteins, M. K. Jain, P. Singh, S. Roy, and R. Bhat, Biochemistry, 57(26), 3830–3848 (2018).
  3. Resveratrol interferes with an early step in the fibrillation pathway of human lysozyme and modulates it towards less-toxic, off-pathway aggregates, F. K. Zaidi and R. Bhat, ChemBiochem, 19, 159-170 (2018).
  4. The α10 helix of DevR, the Mycobacterium tuberculosis dormancy response regulator, regulates its DNA binding and activity, A. Vashist, D. Prithvi Raj, U. D. Gupta, R. Bhat, J. S. Tyagi, FEBS J., 283(7), 1286-99 (2016).
  5. Impact of structural stability of cold adapted Candida antarctica lipase B (CaLB) in relation to pH, chemical and thermal denaturation, G. Rabbani,  E. Ahmad,  M. V. Khan,  M. T. Ashraf,  R. Bhat and   R. H. Khan, RSC Adv., 5, 20115-20131 (2015).
  6. Significantly enhanced heme retention ability of myoglobin engineered to mimic the third covalent linkage by non-axial histidine to heme (vinyl) in Synechocystis hemoglobin, S. Uppal, S, Salhotra, N. Mukhi, F. K. Zaidi, M. Seal, S. Ghosh Dey, R. Bhat and S. Kundu, J. Biol Chem., 290, 1979-93 (2015).
  7. Modulation of human α-synuclein aggregation by a combined effect of calcium and dopamine, M. Jain and R. Bhat, Neurobiology of Disease, 63, 115-128 (2014).
  8. Polyol osmolytes stabilize native-like cooperative intermediate state of yeast hexokinase A at low pH, P. K. Devaraneni, N. Mishra and R, Bhat, Biochimie, 94, 947-952 (2012).
  9. Stereo-selectivity of human serum albumin to enantiomeric and isoelectronic pollutants dissected by spectroscopy, calorimetry, and bioinformatics,  E. Ahmad, G. Rabbani, N. Zaidi, S. Singh, M. Rehan, M. M. Khan, S. K. Rahman, Z. Quadri, M. Shadab, M. T. Ashraf, N. Subbarao, R. Bhat, and R. H. Khan, PLosOne 6(11), e26186 (2011).
  10. Dissecting the role of critical residues and substrate preference of a fatty acyl-coAsynthetase (FadD13) of Mycobacterium tuberculosis, G. Khare, V. Gupta, R. K. Gupta, R. Gupta, R. Bhat and A. K. Tyagi, PLoS One, 4(12), e8387 (2009).
  11. Differential behavior of missense mutations in the intersubunit contact domain of the human pyruvate kinase M2 isozyme, K. Akhatar, V. Gupta, A. Koul, N. Alam, R. Bhat, and R.N.K. Bamezai, J. Biol. Chem., 284, 11971-11981 (2009).
  12. Directed evolution of an anti-human red blood cell antibody, A. Gupta, V. K. Chaudhary, and  R. Bhat,  mAbs, 1, 1-13(2009)
  13. Inhibition of Protein Aggregation: Supramolecular Assemblies of Arginine Hold the Key, Das U, Hariprasad G, Ethayathulla AS, Manral P, Das TK, Pasha S, Mann A, Ganguli M, Verma AK, Bhat R, Chandrayan SK, Ahmed S, Sharma S, Kaur P, Singh TP, Srinivasan A., PLoS One. 2(11), e1176 (2007).
  14. CHIP chaperones wild type p53 Tumor suppressor protein, V. Tripathi, A. Ali, R.  Bhat, and U. Pati, J. Biol. Chem., 282, 28441-28454 (2007).
  15. Chemical chaperone mediated protein folding: Stabilization of P22 tailspike folding intermediates by glycerol, R. Mishra, R. Bhat, and R. Seckler, Biol. Chem., 388, 797-804 (2007).
  16. Stabilization of yeast hexokinase A by polyol osmolytes: Correlation with the physicochemical properties of aqueous solutions, A. Tiwari and R. Bhat, Biophys. Chem., 124, 90-99 (2006).
  17. Efficient refolding of aggregation prone citrate synthase by polyol osmolytes: How well are folding and stability aspects coupled? R. Mishra, R. Seckler, and R. Bhat J. Biol. Chem., 280, 15553-15560 (2005).
  18. Ultra–rapid mixing experiments shed new light on the characteristics of the initial conformational ensemble during the folding of Ribonuclease A, E. Welker, K. Maki, M. C. R. Shastry, D. Juminaga, R. Bhat, H. A. Scheraga, and H. Roder, Proc. Natl. Acad. Sci.(USA),101, 17681-17686 (2004).
  19. 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, D. Prasanna Kumar, A. Tiwari and R. Bhat, J. Biol. Chem., 279, 32093-32099 (2004).
  20. Thermal inactivation of protective antigen of Bacillus anthracis and its prevention by polyol osmolytes, S. Singh, A. Singh, M. A. Aziz, S. A. Waheed, R. Bhat* and R. Bhatnagar, Biochem. Biophys. Res. Commun., 322, 1029-1037 (2004).
  21. The osmoprotectants glycine and its methyl derivatives prevent the thermal inactivation of protective antigen of Bacillus anthracis, S. Singh, M. A. Aziz, P. Khandelwal, R. Bhat*, and R. Bhatnagar, Biochem. Biophys. Res. Commun., 316, 559-564 (2004).
  22. Why is trehalose an exceptional protein stabilzer?: An analysis of the thermal stability of proteins in the presence of the compatible osmolytetrehalose, J. K. Kaushik and R. Bhat, J. Biol. Chem., 278, 26458-26475 (2003).
  23. Proline isomerization in bovine pancreatic ribonuclease A. 2. Folding conditions, R. Bhat, W. J. Wedemeyer, and H. A. Scheraga, Biochemistry, 42, 5722-5728 (2003).
  24. Gln277 and Phe554 residues are involved in thermal inactivation of protective antigen of Bacillus anthracis, S. Singh, N. Ahuja, V. Chauhan, E. Rajasekaran, S. M. Waheed, R. Bhat*, and R. Bhatnagar, Biochem. Biophys. Res. Commun., 296, 1058-1062 (2002).
  25. Effect of pH on stability of anthrax lethal factor: Correlation between denaturation and activity, P. Gupta, S. Singh, A. Tiwari, R.Bhat* and R. Bhatnagar, Biochem. Biophys. Res. Commun., 284, 568-573 (2001).
  26. An efficient and cost-effective procedure for preparing samples for Differential Scanning Calorimetry Experiments, A. Tiwari, D. Prasanna Kumar, and R. Bhat, Anal. Biochem., 284, 406-408 (2000).
  27. A mechanistic analysis of the increase in the thermal stability of proteins in aqueous carboxylic acid salt solutions, J.K. Kaushik and R. Bhat, Protein Sci., 8, 222-233 (1999).
  28. A comparative investigation of differential scanning calorimetric transitions of O2- evolving photosystem II enriched menbranes isolated from beet spinach (Beta vulgaris palanga) leaves and greened cucumber (Cucumissativus) cotyledons. I.B. Jha, S.R. Mishra, R. Bhat and P. Mohanty, Ind. J. Expt. Biol., 37, 61-65 (1999).
  29. Thermal stability of proteins in aqueous polyol solutions : Role of the surface tension of water in the stabilizing effect of polyols, J.K. Kaushik and R. Bhat, J. Phys. Chem. B, 102, 7058-7066 (1998).
  30. Effect of a mixed stabilizer-denaturant system on the stability of enzyme activity at high temperatures: lysozyme as a model, Y. Sangeeta Devi, U.B. Nair and R. Bhat, in Stability and Stabilization of Biocatalysts, (A. Ballesteros, F.J. Plou, J.L.Iborra, and P.J.Halling, eds.),Elsevier (1998), Progress in Biotechnology, 1(15), 263-268 (1998).
  31. Thermostabilization of Protective Antigen- The binding component of anthrax lethal toxin, C. Radha, P. Salotra,  R. Bhat* and R. Bhatnagar, J. Biotechnol., 50, 235-242 (1996).
  32. Effect of solvent additives on the thermal stability of insulin, V.Gupta and R.Bhat, in Perspectives on Protein Engineering and Complementary Technologies (M.J.Geisow and R.Epton, Eds.), Mayflower Worldwide, UK, pp 209-212, (1995).
  33. Steric exclusion is the principal source of the preferential hydration of proteins in the presence of polyethylene glycols, R.Bhat and S.N.Timasheff, Protein Science, 1,1133-43 (1992).
  34. Thermodynamic studies on the interaction of some ureas and salts with micellar  Triton-X-100 in aqueous solutions, V.K.Sharma and R.Bhat, Thermochim. Acta, 160, 315 (1990).
  35. Why preferential hydration does not always stabilize the native structure of globular proteins, T.Arakawa, R.Bhat and S.N.Timasheff, Biochemistry, 29, 1924 (1990).
  36. Preferential interactions determine protein solubility in three component solutions: The magnesium chloride system, T.Arakawa, R.Bhat and S.N.Timasheff, Biochemistry, 29, 1914 (1990).
  37. Thermodynamics of some nucleic acid bases and nucleosides in water and their transfer to aqueous glucose and sucrose solutions at 298.15K, N.Kishore, R.Bhat and J.C.Ahluwalia, Biophys. Chem, 33, 227 (1989).
  38. Calorimetric studies on the interaction of sugars and polyols with the nonionic surfactant Triton-X-100 in aqueous solution, V.K.Sharma and R.Bhat, Thermochim. Acta, 138, 359 (1989).
  39. Thermodynamic studies of transfer of some amino acids and peptides from water to aqueous glucose and sucrose solutions at 298.15K, R. Bhat, N.Kishore and J.C.AhluwaliaJ. Chem. Soc. Faraday Trans. I, 84, 2651 (1988).
  40. Temperature dependence of enthalpies and heat capacities of micellization of sodium dodecyl sulfate in water, V.K.Sharma, R.Bhat and J.C.Ahluwalia, J. Colloid Interface Sci., 115, 396 (1987).
  41. Effect of calcium chloride on the conformation of proteins: Thermodynamic studies of some model compounds, R.Bhat and J.C.Ahluwalia, Int. J. Peptide Protein Res., 30, 145 (1987).
  42. Calorimetric studies on the enthalpies and heat capacities of micellization for Triton-X-100 in water, V.K.Sharma, R.Bhat  and J.C.Ahluwalia, J. Colloid Interface Sci., 112, 195 (1986).
  43. Partial molar heat capacities and volumes of transfer of some amino acids and peptides from water to aqueous sodium chloride solutions at 298.15 K, R.Bhat and J.C.Ahluwalia, J. Phys. Chem., 89, 1099 (1985).

Other Publications:

Prof. J. C. Ahluwalia-Achievements of a lifetime: From thermodynamics of model compounds to proteins, R. Bhat and S. Deep, J. Proteins and Proteomics,  3, 75-78  (2012).

* Co-corresponding author

Total Citations: 2702; h-index: 21; i10-index: 30; Average Citations per paper: 63 (Source: Google Scholar)             --updated 18-07-2018

 

Invited Lectures/participation in conferences

  1. Comparative analysis of the conformation, aggregation, interaction and fibrillation of human α, β, and γ synuclein proteins, International Conference on Intrinsically Disordered Proteins: Forms, Functions, and Diseases (IDP-2017), IISER, Mohali, Dec. 12, 2017.
  2. Cosolvent-assisted protein stability, folding and amyloid inhibition, Protein interest group meeting, Jawaharlal Nehru Institute of Advanced Studies, JNU, New Delhi, Nov. 25, 2017
  3. Data analysis and applications of Circular Dichroism Spectroscopy, in the workshop “Circular Dichroism Spectroscopy and its Research Applications” organized by Advance Instrumentation Research Facility (AIRF), JNU, New Delhi, 24th Nov. 2017
  4. Differential Scanning Calorimetry and Isothermal Titration Calorimetry: Principle and applications for monitoring biomolecular stability and interactions, Centre for Research in Basics Sciences (CIRBSc), Jamia Millia Islamia, New Delhi, Nov. 3, 2017.
  5. From order to disorder- a paradigm shift in Structural Biology: Use of polyphenols in suppression of protein aggregation and amyloid formation, National Conference on Biotechnology and Environment, Department of Biotechnology, Jamia Millia Islamia, New Delhi, 11th April, 2017
  6. Interaction of the polyphenol EGCG with globular human recombinant lysozyme and intrinsically disordered brain protein γ-Synuclein using calorimetric and spectroscopic tools, 11th National Conference on Advances in Chemical Sciences and Thermodynamics, University of Jammu, Jammu, December 3, 2016.
  7. Microcalorimetry and its application in monitoring biomolecular stability and interactions, Workshop on “Advanced Techniques in Protein Design and Engineering”, Centre for Protein Science, Design, and Engineering, IISER Mohali, 17th March, 2016.
  8. Challenges in the in vitro refolding and prevention of aggregation of proteins, Workshop on “Advanced Techniques in Protein Design and Engineering”, Centre for Protein Science, Design, and Engineering, IISER Mohali, 17th March, 2016.
  9. Protein Structure and Folding- A Paradigm Shift in Structural Biology, Valedictory Lecture, Summer Undergraduate Research Programme,Ambedkar Centre for Biomedical Research (ACBR), Univ. of Delhi, July 15, 2015
  10. Suppression of amyloid fibril formation of recombinant human lysozyme by the red wine polyphenol resveratrol, F. K. Zaidi and R. Bhat, Asian Biophysics Association Conference, ABA- 2015, Hangzhou, China, May 9-12, 2015.
  11. Chemistry Meets Biology: Applications for Industry and Medicine, RASAGYA-2015, Sri Venkateswara College, University of Delhi South Campus, New Delhi, Feb. 27, 2015.
  12. Osmolyte effect on protein stability, folding and aggregation: Globular vs. intrinsically disordered protein human brain α-synuclein, M.K. Jain and R. Bhat, Bioworld 2014, Kusuma School of Biological Sciences, IIT Delhi, Dec.13, 2014.
  13. Folding of proteins and challenges in preventing misfolding and aggregation of proteins, Academic Staff College, JamiaMilliaIslamia, New Delhi, May 16, 2014.
  14. Understanding solvent-mediated protein stability effects: spectroscopic and calorimetric studies on glucose oxidase in the presence of polyols, N. K. Mishra and Rajiv Bhat, 10th International Conference on Protein Stabilization, Stresa, Italy, May 7-9, 2014
  15. Protein folding, aggregation and disease: Role of chemical chaperones, Annual Conference on Frontiers in Biomedical Research, Ambedkar Centre for Biomedical Research (ACBR), University of Delhi, April 16, 2014.
  16. Protein stability, folding, aggregation and disease: Issues and challenges, Indian Science Congress, University of Jammu, March 4, 2014.
  17. Cosolvent-mediated stability and folding of proteins and modulation of protein aggregation: Globular vs. intrinsically disordered proteins, 38th Annual Indian Biophysical Society Symposium on Molecular Architecture, Dynamics and Assembly in Living Systems, Saha Institute of Nuclear Physics, Kolkata, March 9, 2014.
  18. Protein Structure, stability, folding and disease: Issues and challenges, Academic Staff College, JamiaMilliaIslamia, May 23, 2013.
  19. Understanding solvent-mediated protein stability and folding and its relation to conformational diseases, in Ramachandran Manifestation: Peptide to Proteome; commemorating 50 years of Ramachandran Plot, Sri Venkateswara College, University of Delhi, South campus, March 15, 2013.
  20. One day workshop and discussion meeting on Synthetic Biology- Building the foundations of biological engineering in India, JNU, New Delhi, Chaired a Session, December 21, 2012.
  21. Calorimetry of Biomolecules: Monitoring biomolecular stability and interactions, Refresher course in Physics. Academic Staff College, JNU, September 13, 2012.
  22. Protein folding, aggregation and diseases, Refresher course in Biotechnology, Academic Staff College, JNU, July 27, 2012.
  23. Structural genomics and beyond: Stabilizing model globular proteins and instrinsically disordered proteins implicated in disease, National Conference on Omics for Biotechnology (NCOB-2012), Central University Rajasthan, Kishangarh, Feb. 22-23, 2012
  24. Determinants in protein folding and controlling misfolding and aggregation of proteins implicated in disease, Refresher course in Life Sciences, Academic Staff College, JNU, Jan.25, 2012.
  25. Indian Biophysical Society Meeting, University of Madras, Chennai, Jan. 19-21, 2012, as Secretary, IBS.
  26. Calorimetric studies of the effect of organic osmolytes on the thermodynamic stability of enzymes: Hexokinase A and glucose oxidase as case studies, Plenary Lecture, National Conference on Thermodynamics of Chemical and Biological Systems, M. D. University, Rohtak, Nov. 2, 2011.
  27. Effect of Stress osmolytes on the stability, folding and aggregation of proteins, One day Symposium on “Proteins Shaped his Life-in Vinod’s memory, CDRI, Lucknow, August 24, 2011.
  28. Protein folding, stability and conformational diseases, Department of Animal Biotechnology, CCS Haryana Agricultural University, Hisar, March 19, 2011.
  29. Understanding protein folding and stability aspects and their relationship to conformational diseases, National Symposium on Current Trends in Biochemical, Biomedical and Environmental Sciences, Department of Biochemistry, Aligarh Muslim University, Aligarh, February 22, 2011. Guest of honour and Keynote speaker.
  30. Chemistry and Biology of environmental adaptation: How do biomolecules cope up, Symposium on Sustainable energy and Environment, Department of Chemistry, Ramjas College, University of Delhi, January 28, 2011
  31. Chaired a Technical session on Biosensor development, International Interdisciplinary Conference on Nanobiotechnology-Interface between Physics and Biology, JamiaMilliaIslamia, New Delhi, Dec. 2-4, 2010.
  32. Protein stability, folding and disease: Issues and Challenges, Biotechnica Chandigarh 2010, Panjab University, Chandigarh, Nov. 17, 2010
  33. Understanding solvent effects on the stability, folding and aggregation of proteins, Indo-Swiss Symposium on Bioinformatics, IIT Delhi, October 26, 2010. Also Chaired a technical session.
  34. Protein stability, folding and disease: Issues and challenges, Institute of Biological Sciences, University of Malaya, Kuala Lumpur, Malaysia, May 5, 2010.
  35. Protein folding and disease, School of Biotechnology, Gautam Buddha University, Greater Noida, April 20, 2010.
  36. How does solvent environment affect the stability, refolding and aggregation of proteins? Dec.17, 2009, National Centre for Biological Sciences, Bangalore.
  37. Unraveling solvent effects on protein structure and stability using spectroscopic and calorimetric tools, Interdisciplinary Science Conference -2009: Interface between Chemistry and Biology, Centre for Interdisciplinary Research in Basic Sciences, JamiaMilliaIslamia, Oct. 8, 2009 (invited Lecture and Session Chairman).
  38. Protein structure and folding: New insights, Workshop on Proteomics, Genomics and Bioinformatics, Supercomputing facility for Bioinformatics (SCFBio), IIT Delhi, October 3, 2009.
  39. Solvent effect on protein stability and aggregation, School of Chemistry, University of Hyderabad, Hyderabad, September 10, 2009.
  40. Protein structure and stability, 11th Refresher course in Biotechnology, Academic Staff College, JNU, New Delhi, July 28, 2009.
  41. Protein folding, aggregation and disease, 11th Refresher course in Biotechnology, Academic Staff College, JNU, New Delhi, July 30, 2009.
  42. Correlation between solvent-mediated thermodynamic stability of proteins and refolding efficacy, Gordon Research Conference on Proteins, Holderness School, New Hampshire, USA, June 21-26, 2009.
  43. Protein Structure, folding, and aggregation- An overview, Summer School, School of Life Sciences, JNU, New Delhi, June 8, 2009.
  44. How does solvent environment affect the structure, stability and folding of proteins?, Indo-French Seminar on Biomolecular Chemistry, Department of Chemistry, University of Delhi, March 4, 2009.
  45. Stabilizing Proteins and Protein Assemblies using Solvent-Mediated Approach: Issues and Challenges, Workshop on Proteomics and Bioinformatics, NDRI, Karnal, February 18, 2009.
  46. Why study protein folding?: Old issues and new challenges, Trends in Biosciences Symposium, JamiaMilliaIslamia, New Delhi, February 12, 2009.
  47. Understanding solvent-mediated protein stability effects: spectroscopic and calorimetric studies on glucose oxidase in the presence of polyols, National Symposium on Cellular and Molecular Biophysics, CCMB, Hyderabad, January 22-24, 2009.
  48. Recent challenges in investigating protein folding, Refresher course in Life Sciences, Academic Staff College, JNU, January 16, 2009.
  49. Principle and applications of stopped-flow spectroscopic techniques, National Workshop on Advanced Analytical Instrumentation and Applications-2009, JNU, New Delhi, January 5-7, 2009.
  50. Calorimetric investigation of stabilization of the two-domain protein yeast hexokinase A by osmolytes of the glycine series, 6th Annual Conference on Applications of Biocalorimetry (abc6), Heidelberg, Germany, July 7-10, 2008.
  51. Enhancing refolding yields of proteins using small molecule chemical chaperones, BIT’s 1st Annual Protein/Peptide Conference (PepCon 2008), Shenzhen, China, April 22-24, 2008.
  52. Protein folding and aggregation- An overview, Workshop on Protein Folding and Bioinformatics, , Bose Institute, Kolkata , March 4-5, 2008.
  53. Protein-solvent interactions and protein stability: The intriguing story of glucose oxidase, JNU Science Festival 2008, February 29- March 1, 2008.
  54. Issues and Challenges in investigating folding of proteins, Symposium on Recent Trends in Biosciences, Dept. of Biosciences, JamiaMilliaIslamia, New Delhi, February 13, 2008.
  55. Recent advances in Protein folding, Refresher Course in Biotechnology, Academic Staff College, JNU, August 7, 2007.
  56. Protein Folding, aggregation and disease, Department of Chemistry, IIT Delhi, March 5, 2007.
  57. Trends in Biotechnology, 57th Orientation Course, Academic Staff College, JNU, January 8, 2007.
  58. Calorimetric investigation of protein-solvent interactions: Mechanism of stabilization of hexokinase A by polyols and carboxylic acid salts, Plenary Lecture, National Conference on Thermodynamics of Chemical and Biological Systems. Guru Nanak Dev University, Amritsar, December 28-30, 2005.
  59. Basic principles of protein folding and the role of chemical chaperones in the folding and stability of proteins, Refresher course in Biotechnology, Academic Staff College, JNU, New Delhi, September 8 and 12, 2005.
  60. Current advances in protein folding and stability, Department of Biomedical Sciences, Acharya Narendra Dev College, University of Delhi, South Campus, September 14, 2004.
  61. Solvent environment plays a critical role in the stability of protein structure and function, 18th Symposium of The Protein Society, San Diego, USA, August 14, 2004.
  62. Biomolecular Interactions and Protein Folding, Supercomputing facility for Bioinformatics and Computational Biology, IIT, Delhi, July 3, 2004.
  63. Environmental factors in protein structure formation and disease, 9th Refresher course in Environmental Sciences, Academic Staff College, JNU, New Delhi, March 11, 2004.
  64. Protein Structure and Folding, Biophysics Symposium, Sri Venkateswara College, Delhi University South Campus, New Delhi, February 28, 2004.
  65. Biophysical Studies on Protein folding and stability - I & II, 5th Refresher Course in Physics, Academic Staff College, JNU, New Delhi, January 27, 2004.
  66. Protein aggregation and disease- Current advances, 9th Refresher Course in Life Sciences, Academic Staff College, JNU, New Delhi, January, 2004.
  67. How does solvent environment affect the folding and stability of proteins? Guha Research Conference, ChalsaSinclairs Retreat, North Bengal, Dec. 25-29, 2003.
  68. Solvent mediated stabilization of proteins: Thermodynamic basis for the stabilization, Central Food Technological Research Institute, Mysore, June 20, 2003.
  69. Protein structure, folding and stability, Academic Staff College, JNU, New Delhi, January 6, 2003.
  70. Protein aggregation and disease: Citrate synthase as a model, 4th Annual Symposium on Frontiers in Biomedical Sciences, Dr. B.R. Ambedkar Centre, University of Delhi, Delhi, May 13-15, 2003.
  71. Why is trehalose an exceptional protein stabilizer: Thermodynamic basis for its stabilizing effect, Symposium on “At the Interface of Physics and Biology”, School of Physical Sciences, JNU, New Delhi, Mar. 5-6, 2003.
  72. Delivered a Series of Invited Lectures for M.Sc. students at Department of Biochemistry, University of Delhi, South campus on “Biophysical techniques” and “Structural Biology” in 1997, 1998, 1999, 2002, 2003, 2004.
  73. First Indian Symposium of “The Protein Society”, I.I.T., Mumbai, Oct. 18-20, 2002.
  74. Participated in the NIH workshop on Computational Biology Tools for Windows, Cornell University, Ithaca, NY, USA, Nov. 16-17, 2000.
  75. Symposium on “Genes to Proteins and to Biological Function”, Cornell University, Ithaca, NY, USA, Oct. 5-6, 2000.
  76. XIII International Biophysics Congress, New Delhi, Sept. 19-24, 1999.
  77. International Symposium on “Stability and Stabilization of Biocatalysts” Cordoba, Spain, April. 19-22, 1998.

Chairing of Conference/Symposia sessions

  1. Chaired  a session on Structural Biology, Biochemistry and Proteomics in”86th Annual Meeting of Society of Biological Chemists (India), JNU, New Delhi, Nov. 19, 2017.
  2. Chaired a session in the National Conference on Protein Structure and Dynamics in Health and Agriculture organized by Department of Biosciences and Centre for Interdisciplinary Research in Biosciences under the aegis of Protein Society, Jamia Millia Islamia, New Delhi, November 3, 2017.
  3. Chaired a session on “Integrative Biology” at the In-house Symposium of ICGEB, New Delhi (ISIN-2017), July 18, 2017.
  4. Chaired a session in the International Biological Engineering Meeting held at Jawaharlal Nehru University, New Delhi, March 26-28, 2017.
  5. Chaired a Technical Session in 11th National Conference on Advances in Chemical Sciences and Thermodynamics, University of Jammu, December 3, 2016.
  6. Chaired a session in 12th Annual Conference of the International Society for Heart Research, JNU, March 14, 2015.
  7. Chaired a Session on Protein folding and diseases, National Symposium on Biophysics and Golden Jubilee Meeting of Indian Biophysical Society, Jamia Millia Islamia, New Delhi, February, 16, 2015.
  8. Chaired a Session on Nanoelectronics in International Conference on Recent Advances in Nanosciences and Nanotechnology (ICRAN-2014), Dec. 16, 2014
  9. Chaired a Session in the Symposium “Bioworld 2014”, Kusuma School of Biological Sciences, IIT Delhi, Dec.13, 2014.
  10. Chaired a session on Protein folding in National Conference on Recent Trends in     Protein Structural Biology, Jamia Millia Islamia, December 16, 2013
  11. Chaired the Session on Protein folding and interactions on 5-1-2013 in the Symposium on Biomolecules in motion; theory and Simulations in JNU, New Delhi from Jan 4-6, 2013.
  12. Chaired a session in the DBT-BUILDER and Symbiosis International University joint one day workshop/meeting on Synthetic Biology, 21-12-2012.         
  13. Special Session on Alumni talks in the Golden Jubilee Symposium of Chemistry Dept. of IIT, Delhi on New Directions in Chemical Sciences, Dec. 7-9, 2012.
  14. International Interdisciplinary Science Conference (I-ISc) on Protein folding a diseases in JamiaMilliaIslamia, New Delhi, Dec. 8-10, 2012.
  15. Session on Functional Genomics in National Conference on Omics for Biotechnology (NCOB-2012), Central University Rajasthan, Kishangarh, Feb. 22, 2012.
  16. Session “Molecules and Diseases” in “5th Annual Symposium on Frontiers in Molecular Medicine”, Special Centre for Molecular Medicine, JNU, New Delhi, Feb. 18, 2012.
  17. Technical Session in the National Conference on Thermodynamics of Chemical and Biological Systems, M. D. University, Rohtak, Nov. 2, 2011.
  18. Indian Proteomics Conference, IPCON-2011, Session on Disease Proteomics (non- communicable diseases), JNU, New Delhi, April 5, 2011.
  19. Indo- French Seminar on Biomolecular Chemistry, Technical Session III, Department of Chemistry, University of Delhi, March 4, 2009.
  20. JNU-Uppsala University joint symposium on Frontiers in Molecular medicine,Scientific Session II: Protein: Structure and Function, February 13, 2009.
  21. National Symposium on Cellular and Molecular Biophysics, Session 4: Protein folding and aggregation, CCMB, Hyderabad, January 23, 2009.

Administrative and other academic responsibilities

Dean School of Biotechnology 2009-11
Director of Admissions, JNU, 2011-2013
Member Selection committee for Faculty/Scientists at University of Delhi, National Institute of Immunology, Institute of Genomics and  Integrative Biology, Regional Centre for Biotechnology, New Delhi, Guru Nanak Dev University, Amritsar, CFTRI, Mysore, University of Raipur.
Chairman, Selection Committee for Faculty and Scientists, National Institute of Immunology, 2016.
Chairman, Committee to Review Admission Policy of JNU 2012.
Chairman, Committee to examine 5 year Admissions data and to look into the weightage for viva voce marks for admission in JNU, 2012.
Member, Board of Studies, Regional Centre for Biotechnology, Faridabad, 2017-.
Member, Special Committee, School of Life Sciences, JNU, 2017-2020.
Member, Committee to look into modalities for conducting JNU Entrance Examination in December, 2017.
Member of Committee for looking into selection committee criteria and eligibility qualifications for direct recruitment of teachers in JNU, 2011.
Member Committee for preparing “JNU Vision 2020 and Beyond” 2011
Member Advisory Committee, Communication and Information Services Centre, JNU 2016-18
Member, INSA-IUPAB National Committee on Biophysics, 2013-2018
Member, Khorana Scholars Programme, selection committee, Indo-US Science and Technology Forum, Delhi, 2013, 2014, 2016, 2017, 2018.
Member Academic Audit Committee for JNU affiliated institutions-CCMB, Hyderabad, 2014
Member Advisory Committee, Advanced Instrumentation Research Facility, JNU 2014-2016; 2017-2020.
Member Board of Studies, Regional Centre for Biotechnology, Faridabad, 2017-
Member Research Area Panels (RAP), National Institute of Immunology, New Delhi, 2018-
Member Academic Committee CDRI, Lucknow, 2014-2016
Member Academic Committee, ICGEB, New Delhi 2009-2011 and 2016-2018.
Member Academic Committee, CCMB, Hyderabad, 2014-2016
Member Academic Committee, Institute of Microbial Technology (IMTech), Chandigarh, 2013-2015
Member Expert Committee to evaluate Translational Health Sciences and Technology Institute (THSTI), Gurgaon for affiliation to JNU, 2013
Member Standing Committee on Recognized Institutions 2011-2013
Member Task force on Star College Scheme of DBT, Govt. of India, 2011-2013
Chairman, House Allotment Committee (PDF), JNU, 2016-2018
Member Hub Advisory Committee, Transdisciplinary Research Cluster, JNU 2014-
Member Special Committee, Special Centre for Nanosciences, 2013-2015; 2015-2017
Member Special Committee, School of Computational and Integrative Sciences 2015-2018
Member, Centre Committee, Centre for Community Medicine and Social Health, 2014-2016.
Member, Institutional Ethics Review Board (IERB), JNU, 2014-16
Member Board of Management and Committee of Studies, Interdisciplinary Biotechnology Unit, Aligarh Muslim University
Member Committee of Studies, Centre for Interdisciplinary Research in Basic Sciences 2012-2016
Member Advisory Committee, Department of Biotechnology, Guru Nanak Dev University, Amritsar, 2013-2015.
Member Advisory Committee, Biotechnology programme, BHU, Varanasi, 2015-2017
Member, Doctoral committee, Faculty of Interdisciplinary Studies, Jamia Hamdard, 2014-
Coordinator M.Sc. Biotechnology Paper setting for a number of years since 1990
Coordinator Ph.D. Biotechnology Paper setting for a number of years since 1990

 

 

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