PG
Purnananda Guptasarma
Indian Institute of Science Education and Research (IISER) Mohali, Instituteof Microbial Technology, University of Cambridge, Centre for Cellular and Molecular Biology CSIR
0000-0002-4801-3180
Employment
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Indian Institute of Science Education and Research (IISER) Mohali Professor, Professor & Head (2012-2015), Professor & Dean Research (2015-2018)2010 - Present
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Instituteof Microbial Technology Scientist, Senior Scientist, Principal Scientist, Senior Principal Scientist1996 - 2010
Education
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University of Cambridge Wellcome Trust International Research Fellow1994 - 1996
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Centre for Cellular and Molecular Biology CSIR Ph.D Life Sciences (Molecular Biophysics and Biochemistry)1988 - 1993
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Birla Institute of Technology and Science Integrated M.Sc (Hons) Biological Sciences1983 - 1988
Projects & Funding
Projects & funding information is unavailable.
Publications (90)
- Exploring differential interactional preferences of enzyme-bearing dockerins for cohesin domains in the Clostridium thermocellum cellulosome Save
- Transformation of Starch into an Equilibrium Pool of Glucose and Small Maltosaccharides by a Hyperthermophilic Enzyme Exhibiting Coupled (Exo)Amylase-Glucanotransferase Functions Save
- Stationary phase KCl levels trigger changes in Dps conformation to facilitate its partitioning between reversibly-aggregated deposits and Dps-DNA condensates Save
- Differences in activities of domain-swapped chimeras of two homologous hyperthermophile exo-amylase-cum-glucanotransferase GH57 enzymes indicates that a glucan-binding DUF influences donor substrate specificity Save
- Dissecting Triple Emission from a Fluorescent Protein Save
- E. coli cells advance into phase-separated (biofilm-simulating) extracellular polymeric substance containing DNA, HU, and lipopolysaccharide Save
- E. colicells advance into phase-separated (biofilm-simulating) extracellular polymeric substance containing DNA, HU, and lipopolysaccharide Save
- ‘Nunchuck’ proteins: Short flexible linkers resist proteolysis by facilitating motions in flanking domains to inhibit the approach of proteases Save
- The bacterial nucleoid-associated proteins, HU and Dps, condense DNA into context-dependent biphasic or multiphasic complex coacervates Save
- Flexible peptide linkers display higher resistance to proteolysis than rigid linkers by facilitating movements that inhibit the approach of proteases Save