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Suman Kundu

goa Biological Sciences

Senior Professor & Director

Biochemistry & Molecular Biology
skundu@goa.bits-pilani.ac.in
0832-2580101

Publications

  1. Shruti Mathur, Sanjeev Kumar Yadav, Kajal Yadav, Shruti Bhat and Suman Kundu (2023) “A novel single sensor hemoglobin domain from the thermophilic cyanobacteria Thermosynechococcus elongatus BP-1 exhibits higher pH but lower thermal stability compared to globins from mesophilic organisms”. International Journal of Biological Macromolecules. In Press.
  2. Gaurav Kumar, Sanjay Kumar Dey, Suman Kundu (2023). “Nitric Oxide and Cardiovascular Diseases: Cardioprotection, Complications and Therapeutics”. In: Ray, A., Gulati, K. (eds). Nitric Oxide: From Research to Therapeutics. Advances in Biochemistry in Health and Disease, vol 22, pp 41-66, Springer, Cham. https://doi.org/10.1007/978-3-031-24778-1_3.
  3. Pushpanjali Dasauni, Nirpendra Singh, Varun Chhabra, Manoranjan Mahapatra, Renu Saxena, Suman Kundu (2022). “Optimization and Identification of Single mutation in Hemoglobin Variants with 2,2,2 trifluoroethanol modified digestion method and nano-LC coupled MALDI MS/MS”. Molecules. 27, 6357.
  4. Chetna Dhembla, Usha Yadav, Suman Kundu and Monica Sundd (2022). “Lipoate protein ligase B primarily recognizes the C8-phosphopantetheine arm of its donor substrate and weakly binds the acyl carrier protein”. Journal of Biological Chemistry. 298, 102203. 
  5. Bharti, H., Singal, A., Saini, M., Cheema, P.S., Raza, M., Kundu, S. and Nag, A. (2022). “Repurposing the Pathogen Box compounds for identification of potent anti-malarials against blood stages of Plasmodium falciparum with PfUCHL3 inhibitory activity”.  Scientific Reports. 12(1):918.
  6. Gaurav Kumar, Manisha Saini, and Suman Kundu (2022). “Therapeutic enzymes as non-conventional targets in cardiovascular impairments: A Comprehensive Review”. Canadian Journal of Physiology and Pharmacology. 100(3):197-209.
  7. Chand, V., Kapoor, A., Kundu, S.*, Nag A.* (2022) “Identification of a peptide that disrupts hADA3-E6 interaction with implications in HPV induced cancer therapy”. Life Sciences. 288:120157.  (*Joint Corresponding Authors)
  8. Khan, M.A., Uppal, S. and Kundu, S.  (2021). “Novel Hemoglobin from Synechocystis sp. PCC 6803: Shedding Light on the Structure-Function Relationship and Its Biotechnological Applications” in Cyanobacteria - Recent Advances in Taxonomy and Applications. 1st ed. Wael N. Hozzein Ed. Intech Open (London, England). ISBN: 978-1-83962-490-2, Doi: 10.5772/intechopen.97699.
  9. Dey, S.K., Saini, M., Dhembla, C., Bhatt, S., Rajesh, A. S., Anand, V., Das, H.K., Kundu. S. (2021).  “Suramin, Penciclovir and Anidulafungin exhibit potential in the treatment of COVID-19 via binding to nsp12 of SARS-CoV-2”. Journal of Biomolecular Structure and Dynamics, 1-17. DOI: 10.1080/07391102.2021.2000498.
  10. Arya, R., Dhembla, C., Makde, R. D., Sundd, M. and Kundu, S. (2021). "An overview of the fatty acid biosynthesis in the protozoan parasite Leishmania and its relevance as a drug target against leishmaniasis". Molecular and Biochemical Parasitology. 246 (750), 111416. https://doi.org/10. 1016/j.molbiopara.2021.111416. 
  11. Kumar, G., Dey, S.K. and Kundu, S. (2021) “Herbs and their bioactive ingredients in cardio-protection: underlying molecular mechanisms and evidences from clinical studies” Phytomedicine. 92, 153753. Corrigendum: 98, 153828.
  12. Dasauni, P., Chhabra, V., Kumar, G. and Kundu, S. (2021).  “Advances in mass spectrometric methods for detection of hemoglobin disorders”. Analytical Biochemistry. 629:114314. https://doi.org/10.1016/j.ab. 2021.114314.
  13. Dhembla, C., Arya, R., Kumar, A., Kundu, S. and Sundd, M. (2021) “L. major apo-acyl carrier protein forms ordered aggregates due to an exposed phenylalanine, while phosphopantetheine inhibits aggregation in the holo-form” International Journal of Biological Macromolecules. 179, 144-153.
  14. Shandilya, M., Kumar, G., Gomkale, R., Singh, S., Khan, M.A., Kateriya, S. and Kundu, S. (2021).  "Multiple putative methemoglobin reductases in C. reinhardtii may support enzymatic functions for its multiple hemoglobins”. International Journal of Biological Macromolecules.   171: 465-479.
  15. Sharma, A., Saini, M., Kundu, S., Thelma B.K. (2020).  "Computational insight into the three-dimensional structure of ADP Ribosylation factor like protein 15, a novel susceptibility gene for rheumatoid arthritis". Journal of Biomolecular Structure and Dynamics. 1-16. DOI:10.1080/07391102.2020. 1860826
  16. Mukhi, N., Kundu, S. and Kaur, J. (2020).  "Coping with stress: Role of Arabidopsis phytoglobins in defence against Sclerotinia sclerotiorum", Journal of Plant Biochemistry and Biotechnology. 29, 804-815.
  17. Kumar, G., Dey, S.K. and Kundu, S. (2020).  “Functional implications of vascular endothelium in regulation of endothelial nitric oxide synthesis to control blood pressure and cardiac functions". Life Sciences 259: 118377. 
  18. Dey, S.K., Saini, M., Prabhakar, P., Kundu, S. (2020). “Dopamine β hydroxylase as a potential drug target to combat hypertension. Expert Opinion on Investigational Drugs. 29(9), 1043-1057.
  19. Uppal, S., Khan, M.A. and Kundu, S. (2020).  “Identification and characterization of a recombinant cognate hemoglobin reductase from Synechocystis sp. PCC 6803”. International Journal of Biological Macromolecules, 162, 1054- 1063.
  20. Uppal, S., Khan, M.A. and Kundu, S. (2020). “Stability and Folding of the Unusually Stable Hemoglobin from Synechocystis is Subtly Optimized and Dependent on the Key Heme Pocket Residues”. Protein & Peptide Letters. 28(2), 164-182.
  21. Dey, S.K, Saini, M., Dhembla, C., Bhatt, S., Rajesh, A.S., Anand, V., Das, H.K. and Kundu, S. (2020).  "Suramin, Penciclovir and Anidulafungin bind nsp12, which governs the RNA-dependent-RNA polymerase activity of SARS-CoV-2, with similar interaction energy as Remdesivir-triphosphate, indicating potential in the treatment of COVID-19 infection". OSF Preprints, DOI: 10.31219/osf.io/urxwh
  22. Kundu, S., Saini, M., Dey, S. K. & Kundu, S. (2020). “Dopamine β hydroxylase: an enzyme with therapeutic potential to combat neural and cardiovascular diseases” in Frontiers in Protein Structure, Function, and Dynamics (eds. Singh, D.B and Tripathi, T.), Springer Nature, Singapore (978-981-15-5529-9, 486507_1_En) 
  23. Agrawal, D.C., Yadav, A., Khan, M.A., Kundu, S.* and Kayastha, A.M.* (2020). “Denaturant induced equilibrium unfolding and conformational transitional studies of germinated fenugreek β-amylase revealed molten globule like state at low pH”. Protein and Peptide Letters. 2020, 27, 1-12.   (*joint corresponding author)
  24. Arya, R., Sharma, B., Dhembla, C., Pal, R.K., Patel, A.K., Sundd, M., Ghosh, B., Makde, R.D. and Kundu, S.(2019). “A conformational switch from a closed apo- to an open holo-form equips the acyl carrier protein for acyl chain accommodation”Biochim Biophys Acta - Proteins and Proteomics. 1867, 163-174
  25. Dasauni, P., Mahapatra, M., Saxena, R. and Kundu, S. (2018). “Refractive index of blood is a potential qualitative indicator of hemoglobin disorder in human”. Journal of Proteins and Proteomics. 9(3), 159-168
  26. Yadav, U., Arya, R., Kundu S. and Sundd, M. (2018) “The 'recognition helix' of the type II Acyl Carrier Protein (ACP) utilizes a 'ubiquitin interacting motif (UIM)' like surface to bind its partners”. Biochemistry 57 (26) 3690-3701
  27. Shankar A, Fernandes J.L., Kaur K, Sharma M, Kundu Sand Pandey GK. (2018). “Rice phytoglobins regulate responses under low mineral nutrients and abiotic stresses in Arabidopsis thaliana”. Plant Cell Environ. 41(1):215-230.  
  28. Sharma, B., Jamdar, S.N., Ghosh, B., Yadav, P., Kumar, A., Kundu, S., Goyal, V.D. and Makde, R.D. (2017). “Active site gate of M32 carboxypeptidases illuminated by crystal structure and molecular dynamics simulations”. Biochim Biophys Acta - Proteins and Proteomics. 1865, 1406-1415
  29. Mukhi, N., Kundu, S., and Kaur, J. (2017) “NO dioxygenase- and peroxidase-like activity of Arabidopsis phytoglobin 3 and its role in Sclerotinia sclerotiorum defense. Nitric Oxide. 68, 150-162 
  30. Punchaichira, T.J., Dey, S.K, Mukhopadhyay, A., Kundu, S., and Thelma, B. K. (2017). “Characterization of SNPs in the dopamine-β-hydroxylase gene providing new insights into its structure-function relationship” Neurogenetics18, 155-168.
  31. Uppal, S., Singh, A.K., Arya, R., Tewari, D., Jaiswal, N., Kapoor, A., Bera, A.K., Nag, A. and Kundu, S. (2016). “Phe28B10 Induces Channel-Forming Cytotoxic Amyloid Fibrillation in Human Neuroglobin, the Brain-Specific Hemoglobin”. Biochemistry 55(49), 6832-6847
  32. Uppal, S., Kumar, A., Shandilya, M., Mukhi, N., Singh, A. K., Kateriya, S., Kaur, J. and Kundu, S. (2016). “Penta- and Hexa-Coordinate Ferric Hemoglobins Display Distinct pH Titration Profiles Measured by Soret Peak Shifts”. Anal. Biochem. 510, 120-128. 
  33. Mukhi, N., Dhindwal, S., Uppal, S., Kapoor, A., Arya, R., Kumar, P., Kaur, J. and Kundu, S. (2016).  “Structural and functional significance of the N- and C-terminal appendages in Arabidopsis truncated hemoglobin”. Biochemistry. 55, 1724-1740.
  34. Jebamercy, G., Durai, S., Prithika, U., Marudhupandiyan, S., Dasauni, P., Kundu, S. and Balamurugan, K. (2016). “Role of DAF-21 protein in Caenorhabditis elegans immunity against Proteus mirabilis infection”. J Proteomics. 145, 81-90.
  35. Vigneshkumar, B., Durai, S., Kundu, S. and Balamurugan, K. (2016).“Proteome analysis reveals translational inhibition of Caenorhabditis elegans enhances susceptibility to Pseudomonas aeruginosa PAO1 pathogenesis”. J Proteomics. 145, 141-152. 
  36. Yadav, R., Kundu, S. and Sarkar, S. (2015). “Drosophila glob1 expresses dynamically and is required for development and oxidative stress”. Genesis. 53, 719-737.
  37. Kumar, A., Arya, R., Makwana, P., Dangi, R., Yadav, U., Surolia, A., Kundu, S. and Sundd, M. (2015). “The structure of the holo-acyl carrier protein of Leishmania major displays a remarkably different phosphopantetheinyl transferase (PPT) binding interface”. Biochemistry. 54, 5632-5645. 
  38. Sharma, S., Kumar, A., Kundu, S.,* and Bandhopadhyay, P.* (2015). “Molecular dynamics simulations indicate that TyrosineB10 limits motions of distal Histidine to regulate CO binding in soybean leghemoglobin”. Proteins: Struc. Func. Bioinform. 83, 1836-1848 (* - joint corresponding author)  
  39. Singh, K., Shandilya, M., Kundu, S.* and Kayastha, A.M.* (2015). “Heat, acid and chemically induced unfolding pathways, conformational stability and structure-function relationship in wheat ?–amylase”. PLoS One. 10(6):e0129203. (*-joint corresponding authors.       
  40. Seal, M., Uppal, S., Kundu, S. and Dey, S.G. (2015). “Interaction of ApoNeuroglobin with Heme-Aβ Complexes Relevant to Alzheimer’s Disease”. J Biol Inorg Chem.20,  563-574.                                 
  41. Uppal, S., Salhotra, S., Mukhi, N., Zaidi, F.K, Seal, M., Ghosh Dey, S., Bhat, R., Kundu, S. (2015). “Significantly enhanced heme retention ability of myoglobin engineered to mimic the third covalent linkage by non-axial histidine to heme (vinyl) in Synechocystis hemoglobin”. J. Biol. Chem. 290, 1979-1993.
  42. Vikash Kumar Dubey and Suman Kundu (2014) “Processing of Recombinant Proteins”In Gene and its Engineering. First Edition Wiley India Pvt. Ltd., New Delhi, India (H. K. Das Ed). Pp. 474-479
  43. Dey, S.K and Kundu, S. (2014) “The Indian Wizard of Biophysics: Remembering G.N. Ramachandran in the International Year of Crystallography”J. Prot. Proteomics5, 65-72.  
  44. Durai, S., Singh, N., Kundu, S.* and Balamurugan, K.* (2014) “Proteomic investigation of Vibrio alginolyticus challenged Caenorhabditis elegans revealed regulation of cellular homeostatis proteins and their role in supporting innate immune system”. Proteomics14,1820-1832.  (*-joint corresponding authors).          
  45. Oshtrakh, M.I., Kumar, A., Alenkina,, I.V., Zakharova, A.P.,  Semionkin, V.A. and Kundu, S. (2014) “Characterization of monomeric soybean leghemoglobin using Mössbauer spectroscopy with a high velocity resolution” Hyp. Interact. 226, 431-438.
  46. Basireddy, S., Uppal, S., Singh, A.K.and Kundu, S. (2013) “An evaluation of potential intrinsically disordered and amyloidogenic regions in hemoglobins”. J. Prot. Proteomics4, 231-248.                   
  47. Jangir, D.K., Kundu, S. and Mehrotra, R. (2013) “Role of minor groove width and hydration pattern on amsacrine interaction with DNA”. PloS One. 8(7):e69933.  
  48. Mukhi, N., Dhindwal, S., Uppal, S., Kumar, P., Kaur, J.and Kundu, S. (2013) “X-ray crystallographic structural characteristics of Arabidopsis hemoglobin 1 and their functional implications”. Biochim. Biophys. Acta1834, 1944-1956.
  49. Kumar, P., Patil, D.N., Chaudhary, A., Tomar, S., Yernool, D., Singh, N., Dasauni, P., Kundu, S. and Kumar, P. (2013) “Purification and biophysical characterization of 11S globulin from Wrightia tinctoria exhibiting hemagglutinating activity”. Prot. Pep. Lett.20, 499-509.
  50. Patil, D.N, Datta, M., Dev, A., Dhindwal, S., Singh, N., Dasauni, P., Kundu, S., Sharma, A. K, Tomar, S. and Kumar, P. (2013) “Structural investigation of a novel N-acetyl glucosamine binding chi-lectin which reveals evolutionary relationship with class III chitinases.”PloS One. 8(5):e63779.
  51. Kishore, D., Kundu, S., andKayastha, A.M. (2012) “Thermal, chemical and pH induced denaturation of a multimeric ?-galactosidase reveals multiple unfolding pathways”.PloS One.7(11):e50380. Doi: 10.1371/journal.pone.0050380.
  52. Arya, R., Sundd, M. and Kundu, S. (2012) “Structural and functional aspects of acyl-coenzyme A binding proteins (ACBPs): a comprehensive review”. J. Prot. Proteomics 3, 61-71.
  53. Jangir, D.K, Dey, S.K., Kundu, S. and Mehrotra, R. (2012) “Assessment of amsacrine binding with DNA using UV-visible, circular dichroism and Raman spectroscopic techniques”. J. Photochem. Photobiol. B. 114, 38-43.
  54. Kapoor, A., Shandilya, M., and Kundu, S. (2011) “Structural insight of dopamine ?-hydroxylase, a drug target for complex traits, and functional significance of exonic single nucleotide polymorphisms” PloS One 6(10): e26509. Doi:10.1371/ journal.pone. 0026509
  55. Jangir, D.K., Charak, S., Mehrotra, R., and Kundu, S. (2011) “FTIR and circular dichroism spectroscopic study of interaction of 5-fluorouracil with DNA”. J. Photochem. Photobiol. B: Biology 105, 143-148.
  56. Oshtrakh*, M.I., Berkovsky, A.L., Kumar, A., Kundu*, S., Vinogradov, A.V., Konstantinova, T.S. and Semionkin, V.A. (2011) “Heme iron states in various oxyhemoglobins probed using Mossbauer spectroscopy with a high velocity resolution”.   Biometals 24, 501-512.
  57. Bisht, N.K., Abbruzzetti, S., Uppal, S., Bruno, S., Spyrakis, F.,Mozzarelli, A., Viappiani*, C. and Kundu*, S. (2011) “Ligand migration and hexacoordination in type 1 non symbiotic rice hemoglobin”. Biochim Biophys. Acta. 1814, 1042-1053.
  58. Oshtrakh*, M.I., Kumar, A., Kundu*, S., Berkovsky, A.L., and Semionkin, V.A. (2011) “Study of human, rabbit and pig oxyhemoglobins using high velocity resolution Mössbauer spectroscopy in relation to their structural and functional variations”. J. Mol. Struc.993, 292-296.
  59. Kumar, S.B., Venkateshwaran, K. And Kundu*, S. (2010) “Alternative Conformational Model of a Seed Protein DeK1 for Better Understanding of Structure-Function Relationship”  J. Prot. Proteomics 1, 77-90. 
  60. Oshtrakh*, M.I., Berkovsky, A.L., Kumar, A., Kundu*, S., Vinogradov, A.V., Konstantinova, T.S. and Semionkin, V.A. (2010) “57Fe Quadrupole Splitting and Isomer Shift in Various Oxyhemoglobins: Study Using Mössbauer Spectroscopy”. Hyp. Interact.197, 301-307. 
  61. Lawit, S.J., Wych, H.M., Xu, D., Kundu, S. and Tomes, D. (2010) “Maize DELLA Proteins dwarf plant8 and dwarf plant9 as Modulators of Plant Development”. Plant Cell Physiol.51, 1854-1868
  62. Yadav, S.C., Jagannadham, M.V. and Kundu*, S (2010) “Equilibrium Unfolding of Kinetically Stable Serine Protease Milin: Presence of Various Active and Inactive Dimeric Intermediates”.Eur  Biophys. J.39, 1385-1396
  63. Jangir, D.K., Tyagi, G., Mehrotra, R., and Kundu, S. (2010) “Carboplatin interaction with calf-thymus DNA: A FTIR spectroscopic approach”. J. Mol. Struc.969, 126-129.
  64. Yadav, S.C., Jagannadham, M.V., Kundu, S., and Jagannadham, M.V. (2009) “A  kinetically stable plant subtilase with unique peptide mass fingerprints and dimerization properties”. Biophys. Chem. 139, 13-23 
  65. Krishnan, A., Verma, S.K., Mani, P., Gupta, R., Kundu, S., and Sarkar, D.P. (2009) “A histidine switch in hemagglutinin-neuraminidase triggers paramyxovirus-cell membrane fusion”.  J. Virol. 83, 1727-1741.
  66. Kumar, A., Uppal, S., and Kundu*, S. (2009) “The Red Goldmine: Promises of Biotechnological Riches” InvitedBook Chapter. Biotechnological Applications, eds. C.S.K. Mishra, India and Dr. Pascale Champagne, Canada. IK Publishing House, Delhi.
  67. Kumar, M.R., Pervitsky, D., Chen, L., Poulos, T., Kundu, S., Hargrove, M.S., Rivera, E.J., Diaz, A., Colón, J.L., Farmer, P.J. (2009) “Nitrosyl hydride (HNO) as an O2 analogue: long-lived HNO adducts of ferrous globins”.Biochemistry48, 5018-5025.
  68. Smagghe, B.J., Hoy, J.A., Percifield, R., Kundu, S., Hargrove, M.S., Sarath, G., Hilbert, J.-L., Watts, R.A., Dennis, E.S., Peacock, W.J., Dewilde, S., Moens, L., Blouin, G.C., Olson, J.S., and Appleby, C.A (2009) “Correlations between oxygen affinity and sequence classifications of plant hemoglobins”. Biopolymers91, 1083-1096.
  69. Smagghe, B.J., Kundu, S., Hoy, J.A., Halder, P., Weiland, T.R., Savage, A., Venugopal, A., Goodman, M., Premer, S., and Hargrove, M.S. (2006) “The role of phenylalanine B10 in plant nonsymbiotic hemoglobins”. Biochemistry45, 9735-9745.
  70. Kundu, S., Blouin, G.C., Premer, S.A., Sarath, G., Olson, J.S., Hargrove, M.S. (2004). “Tyrosine B10 inhibits stabilization of bound carbon monoxide and oxygen in soybean leghemoglobin” Biochemistry43, 6241-6252.
  71. Weiland, T.R., Kundu, S., Trent, J.T., III, Hoy, J.A., Hargrove, M.S. (2004) “bis-Histidyl hexacoordination in hemoglobins facilitates heme reduction kinetics” J. Am. Chem. Soc.126, 11930-11935.
  72. Trent, J.T., III., Kundu, S., Hoy, J.A., and Hargrove, M.S. (2004) “Crystallographic analysis of Synechocystis cyanoglobin reveals the structural changes accompanying ligand binding in a hexacoordinate hemoglobin” J. Mol. Biol.341, 1097-1108.
  73. Hoy, J.A., Kundu, S., Trent, J.T., III., Ramaswamy, S., and Hargrove, M.S. (2004). “The crystal structure of Synechocystis hemoglobin with a covalent heme linkage” J. Biol. Chem.279, 16535-16542
  74. Sundd, M., Kundu, S., Dubey, V.K., and Jagannadham, M.V. (2004). “Unfolding of ervatamin C in the presence of organic solvents: Sequential transitions of the protein in O-state”. J. Biochem. Mol. Biol.37, 586-596
  75. Chowdhury, P.K., Halder, M., Sanders, L., Arnold, R.A., Liu, Y., Armstrong, D.W., Kundu, S., Hargrove, M.S., Song, X., and Petrich, J.W. (2004). “The complex of Apomyoglobin with the Fluorescent Dye, Coumarin 153” Photochem. Photobiol.79, 440-446.
  76. Kundu, S., Trent, J.T., III, and Hargrove, M.S. (2003) “Plants, Humans and Hemoglobins” Trends Plant Sc.8, 387-393. – Review Article
  77. Halder, M., Das, K., Chowdhury, P., Kundu, S., Hargrove, M.S., and Petrich, J.W. (2003) “A comparative femtosecond coherence study of the unligated monomeric hemeproteins Myoglobin and Leghemoglobin”. J. Phys. Chem. B.107, 9933-9938.
  78. Kundu, S. and Hargrove, M.S. (2003). “Distal pocket regulation of ligand binding and stability in soybean leghemoglobin”.Proteins: Struct. Func. Gen. 50, 239-248.
  79. Kundu, S., Premer, S.A., Hoy, J.A., Trent, J.T., III., and Hargrove, M.S. (2003) “Direct measurement of equilibrium constants for high-affinity hemoglobins”Biophys. J.84, 3931-3940.
  80. Nallamsetty, S., Kundu, S., and Jagannadham, M.V. (2003) “Purification and biochemical characterization of a highly active cysteine protease, ervatamin A, from the latex of Ervatamia coronaria”J. Protein Chem. 22, 1-13.
  81. Biswas, S., Chakrabarti, C., Kundu, S., Jagannadham, M.V., and Dattagupta, J.K. (2003) “Proposed amino acid sequence and the 1.63A X-ray crystal structure of a plant cysteine protease, ervatamin B: insights into the structural basis of its stability and substrate specificity”. Proteins: Struct. Func. Gen. 51, 489-497
  82. Chowdhury, P., Kundu, S., Halder, M., Das, K., Hargrove, M.S., and Petrich, J.W. (2003) “Effects of distal pocket mutations on the geminate recombination of NO with leghemoglobin on the picosecond timescale”J. Phys. Chem. B.107, 9122-9127.
  83. Kundu, S., Snyder, B., Das, K., Chowdhury, P., Park, J., Petrich, J.W., and Hargrove, M.S. (2002) “The leghemoglobin proximal heme pocket directs oxygen dissociation and stabilizes bound heme”. Proteins: Struct. Func. Gen.46, 268-277.
  84. Kundu, S., Sundd, M., and Jagannadham, M. V. (2002) “Alcohol and temperature induced conformational transitions in ervatamin B. Sequential unfolding of domains”J. Biochem. Mol. Biol.35, 155-164
  85. Sundd, M., Kundu, S., and Jagannadham, M. V. (2002) “Acid and chemical induced conformational changes of ervatamin B. Presence of partially structured multiple intermediates”J. Biochem. Mol. Biol.35, 143-154
  86. Kundu, S., Sundd, M., and Jagannadham, M. V. (2000) “Purification and characterization of a stable cysteine protease, ervatamin B, with two disulfide bridges from the latex of Ervatamia coronaria”J. Agr. Food Chem. 48, 171-179. 
  87. Sundd, M., Kundu, S., and Jagannadham, M. V. (2000) “Alcohol induced conformational transitions in ervatamin C. An a-helix to b-sheet transition”J. Protein Chem.19, 169-176 
  88. Chakrabarti, R., Kundu, S., Kumar, S., and Chakrabarti, R. (2000) “Vitamin A as an enzyme which catalyzes the reduction of MTT to formazan by vitamin C”. J. Cell. Biochem. 80, 133-138. 
  89. Kundu, S., Sundd, M., and Jagannadham, M. V. (1999) “Structural Characterization of a Highly Stable Cysteine Protease Ervatamin C”Biochem. Biophys. Res. Comm.264, 635-642. 
  90. Chakrabarti, C., Biswas, S., Kundu, S., Sundd, M., Jagannadham, M.V., and Dattagupta, J. K. (1999) “Crystallization and preliminary X-ray analysis of ervatamin B and C, two thiol proteases from Ervatamia coronaria“, Acta Crystallogr. D55, 1074-1075. 
  91. Sundd, M., Kundu, S., Pal, G. P., and Medicherla, J. V.(1998) “Purification and Characterization of a Highly Stable Cysteine Protease from the latex of Ervatamia coronaria”, Biosci. Biotech. Biochem. 62, 1947-1955.

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