biblio

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2014
D. Chand, Panigrahi, P., Ramasamy, S., and Suresh, C. G., “Structure of highly active BSH enzyme with subordinated post-translational excision”, Acta Crystallographica A‐Foundation and Advances, vol. 70, p. C272, 2014.
2015
P. Panigrahi, Chand, D., Mukherji, R., Ramasamy, S., and Suresh, C. G., “Sequence and structure-based comparative analysis to assess, identify and improve the thermostability of penicillin G acylases”, Journal of Industrial Microbiology & Biotechnology, vol. 42, no. 11, pp. 1493-1506, 2015.
D. Chand, Varshney, N. K., Ramasamy, S., Panigrahi, P., Brannigan, J. A., Wilkinson, A. J., and Suresh, C. G., “Structure mediation in substrate binding and post-translational processing of penicillin acylases: Information from mutant structures of Kluyvera citrophila penicillin G acylase”, Protein Science, vol. 24, no. 10, pp. 1660-1670, 2015.
2016
D. Chand, Ramasamy, S., and Suresh, C. G., “Highly active bile salt hydrolase from enterococcus faecalis shows positive cooperative kinetics”, Process Biochemistry, vol. 51, no. 2, pp. 263-269, 2016.
V. Sunder Avinash, Panigrahi, P., Chand, D., Pundle, A., Suresh, C. Gopalan, and Ramasamy, S., “Structural analysis of a penicillin V acylase from pectobacterium atrosepticum confirms the importance of two Trp residues for activity and specificity”, Journal of Structural Biology, vol. 193, no. 2, pp. 85-94, 2016.