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Vasudev, Prema G and Banerjee, Mousumi and Ramakrishnan, C and Balaram, P (2012) Asparagine and glutamine differ in their propensities to form specific side chain-backbone hydrogen bonded motifs in proteins. In: Proteins: Structure, Function, and Genetics, 80 (4). pp. 991-1002.
Samanta, Moumita and Banerjee, Mousumi and Murthy, Mathur RN and Balaram, Hemalatha and Balaram, Padmanabhan (2011) Probing the role of the fully conserved Cys126 in triosephosphate isomerase by site-specific mutagenesis - distal effects on dimer stability. In: FEBS Journal, 278 (11). pp. 1932-1943.
Samanta, Moumita and Banerjee, Mousumi and Murthy, Mathur RN and Balaram, Hemalatha and Balaram, Padmanabhan (2011) Probing the role of the fully conserved Cys126 in triosephosphate isomerase by site-specific mutagenesis - distal effects on dimer stability. In: FEBS Journal, 278 (11). pp. 1932-1943.
Banerjee, Mousumi and Balaram, Hemalatha and Joshi, NV and Balaram, P (2011) Engineered dimer interface mutants of triosephosphate isomerase: the role of inter-subunit interactions in enzyme function and stability. In: Protein Engineering Design and Selection, 24 (5). pp. 463-472.
Banerjee, Mousumi and Balaram, Hemalatha and Balaram, Padmanabhan (2009) Structural effects of a dimer interface mutation on catalytic activity of triosephosphate isomerase.The role of conserved residues and complementary mutations. In: FEBS Journal, 276 (15). pp. 4169-4183.
Gayathri, P and Banerjee, Mousumi and Vijayalakshmi, A and Balaram, Hemalatha and Balaram, P and Murthy, MRN (2009) Biochemical and structural characterization of residue 96 mutants of Plasmodium falciparum triosephosphate isomerase: active-site loop conformation, hydration and identification of a dimer-interface ligand-binding site. In: Acta Crystallographica Section D-Biological Crystallography, 65 (8). pp. 847-857.
Gayathri, P and Banerjee, Mousumi and Vijayalakshmi, A and Azeez, Shamina and Balaram, Hemalatha and Balaram, P and Murthy, MRN (2007) Structure of triosephosphate isomerase (TIM) from Methanocaldococcus jannaschii. In: Acta Crystallographica Section D-Biological Crystallography, 63 (2). pp. 206-220.
