Balaji, PV

Dr. Petety V. Balaji


Phone: +(91-22) 2576 7778
Fax: +(91-22) 2572 7760
E-mail: balaji [at]
Location: Room No. 402, BSBE Building
Lab web page

Research Interest

  • Computational Biology, Bioinformatics, Glycobiology

Academic Background

  • B.Sc.(Physics, Chemistry, Mathematics): University of Mysore
  • M.Sc.(Biochemistry): University of Mysore
  • Ph.D.(Biophysics): Indian Institute of Science


Bioenergetics, Bioinformatics, Molecular Biophysics, Programming for Bioinformatics, Biology (BB101)

Professional Experience

  • Research Associate: Indian Institute of Science, Bangalore
  • Visiting Fellow: Lab. of Mathematical Biology, NCi, NIH
  • Assistant Professor: Biotechnology Center, IIT Bombay
  • Assistant Professor: School of Biosciences and Bioengineering, IIT Bombay
  • Associate Professor: School of Biosciences and Bioengineering, IIT Bombay
  • Professor: Department of Biosciences and Bioengineering, IIT Bombay


  • Kaundinya, C.R., Savithri, H.S., Rao, K.K. and Balaji, P.V. (2018) EpsN from Bacillus subtilis 168 has UDP 2,6-dideoxy 2-acetamido 4-keto aminotransferase activity in vitro. Glycobiology, in press.
  • Pardeshi, P., Rao, K.K. and Balaji, P.V. (2017) Rv3634c from Mycobacterium tuberculosis H37Rv encodes an enzyme with UDP-Gal/Glc and UDP-GalNAc 4-epimerase activities. PLoS ONE, 12, e0175193.
  • Prabhakar, P.K., Srivastava, A., Rao, K.K. and Balaji, P.V. (2016) Monomerization alters the dynamics of the lid region in Campylobacter jejuni CstII: an MD simulation study. J. Biomolec. Struct. Dyn., 34, 778-791.
  • Srivastava, A. and Balaji, P.V. (2015) Molecular events during the early stages of aggregation of GNNQQNY: an all atom MD simulation study of randomly dispersed peptides. J. Struct. Biol.192, 376-391.
  • Prabhakar, P.K., Rao, K.K. and Balaji, P.V. (2014) The Cys78-Asn88 loop region of the Campylobacter jejuni CstII is essential for a2,3-sialyltransferase activity: analysis of the His85 mutants. J. Biochem.156, 229-238.
  • Srivastava, A. and Balaji, P.V. (2014) Interplay of sequence, topology, and termini charge in determining the stability of the aggregates of GNNQQNY mutants: a molecular dynamics study. PLoS ONE9, e96660.
  • Kumar, M. and Balaji, P.V. (2014) CH…pi interactions in proteins: prevalence, pattern of occurrence, residue propensities, location and contribution to protein stability. J. Mol. Model.20, 2136(1-14).

  • Rao, V.S.R., Qasba, P.K., Balaji, P.V., and Chandrasekaran, R. (1998) Conformation of Carbohydrates. Harwood Academic Publishers, The Netherlands.