The two major research areas in my lab are: a) investigating protein folding mechanism using extracellular proteins such as proteases and their protein-based inhibitors implicated in human disease, as model systems and, b) developing protein expression technologies for producing protein-based biotherapeutics. The specifics of our research activity include:

• Investigating folding, mis-folding and functioning of plasma serpins
• Rational re-designing of human alpha-1 antitrypsin and plasminogen activator inhibitor-1 to develop these as improved therapeutic biologics
• Designing & biophysical characterization of fluorescent protein-based biosensors
• Developing technologies for expressing monoclonal antibodies and performing biochemical and biophysical characterization of mAbs.

• Kumar, R., Pinnaka, A.K., and Krishnan, B. (2017) TfoI produced by Tepidimonas fonticaldi PL17, a moderate thermophilic bacterium, is an isoschizomer of MseI. Extremophiles. 21, 523-535.
• Singh, P.K., Solanki, V., Sharma, S., Thakur, K.G., Krishnan, B., and Korpole, S. (2015) The intramolecular disulfide-stapled structure of laterosporulin, a class IId bacteriocin, conceals a human defensin-like structural module. FEBS J. 282, 203-214.
• Budyak, I.L., Krishnan, B., Marcelino-Cruz, A.M., Ferrolino, M.C., Zhuravleva, A., and Gierasch, L.M. (2013) Early folding events protect aggregation-prone regions of a β-rich protein. Structure. 21, 476-485 .
• Krishnan, B., and Gierasch, L.M. (2011) Dynamic local unfolding in the serpin α-1 antitrypsin provides a mechanism for loop insertion and polymerization. Nat. Struct. Mol. Biol. 18, 222-226.
• Krishnan, B., Kulothungan, S.R., Patra, A.K., Udgaonkar, J.B., and Varadarajan, R. (2009) SecB-mediated protein export need not occur via kinetic partitioning. J. Mol. Biol. 385, 1243-1256.