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Sharma, A.K
A.K. Sharma Head Of Department aksbsfbs[at] 91-01332-285657
Areas of Interest
  • Biochemistry, Biophysics, Macromolecular crystallography, Protein biochemestry and structural biology
Professional Background
2012presentAssociate ProfessorDepartment of Biotechnology, IIT Roorkee
20032012Assistant ProfessorDepartment of Biotechnology, IIT Roorkee
19992002Post-doctoral Research AssociateUniversity of North Carolina at Chapel Hill, USA
Educational Details
Ph.D.Biochemistry and BiophysicsAll India Institute of Medical Sciences, New Delhi1999
M.Sc.BiochemistryJiwaji University, Gwalior1993
PHDs Supervised
TopicScholar NameStatus of PHDRegistration Year
Purification and characterization of a trypsin inhibitor from Murraya koenigiiChandan SheeA2003
Studies on some important proteins and peptides from plant and microbial sources.Saurabh AgarwalA2004
. Studies on trypsin inhibitors from plants of Rutaceae family.Deepankar GahlothA2004
Purification and characterization of a trypsin inhibitor from Putranjiva roxburghii.Navneet S ChaudharyA2005
Structural characterization of chitinase.Manali DattaA2006
Studies on glycosidae 1, protease and protease inhibitor from plants of Euphorbiaceae familyGirijesh K PatelA2007
Structure-function studies on miraculin-like proteins.P. Selva KumarA2008
Studies on multifunctional low molecular weight heterodimeric proteinsPrabhat Pratap Singh TomarA2009
Studies on b-glucosidas and acid phosphatase enzymes of hydrolase familyBibekanand KarA2009
Studies on a metal uptake protein from Candidatus Liberibacter asiaticus Nidhi SharmaA2009
Studies on peroxyredoxin antioxidant system from Candidatus Liberibacter asiaticusAnamika SinghA2009
Studies on enzymes involved in purine nucleotide metabolism Preeti VermaA2010
Refereed Journal Papers

1.Verma P, Kar B, Varshney R, Roy P, Sharma AK (2017). Characterization of AICAR transformylase/IMP cyclohydrolase (ATIC) from Staphylococcus lugdunensis. FEBS J. DOI 10.1111/febs14303.

2.Warghane A, Misra P, Bhose S, Biswas KK, Sharma AK, Reddy MK, Ghosh DK (2017). Development of a simple and rapid reverse transcription loop mediated isothermal amplification (RT-LAMP) assay for sensitive detection of Citrus tristeza virus. J Virol. Methods, doi: 10.1016/j.ijbiomac.2017.08.105

3.Kar B, Verma P, den-Haan R, Sharma AK (2017) Characterization of a recombinant  thermostable β-glucosidase from Putranjiva roxburghii expressed Saccharomyces cerevisiae and its use for efficient biomass conversion. Process Biochemistry. DOI:doi:10.1016/j.procbio.2017.08.005

4.Sharma A, Kumar V, Chatrath A, Dev A, Prasad R, Sharma AK, Tomar S, Kumar P. (2017) In vitro metal catalyzed oxidative stress in DAH7PS: Methionine modification leads to structure destabilization and induce amorphous aggregation. Int.J.Biol.Macromol. doi: 10.1016/j.ijbiomac.2017.08.105

5.Kumar P, Kesari P, Dhindwal S, Choudhary AK, Katiki M, Neetu, Verma A, Ambatipudi K, Tomar S, Sharma AK, Mishra G, Kumar P.(2017). A novel function for globulin in sequestering plant hormone: Crystal structure of Wrightia tinctoria 11S globulin in complex with auxin. . Sci Rep. 7(1):4705.

  1. Kar B, Verma P, Patel GK, Sharma AK (2017). Molecular cloning, characterization and in silico analysis of a thermostable β-glucosidase enzyme from Putranjiva roxburghii with significant activity for cellobiose. Phytochemistry, 140, 151-165.
  2. Verma P, Patel GK, Kar B, Sharma AK (2017). A case of neofunctionalization of a Putranjiva roxburghii PNP proteins to trypsin inhibitor by disruption of PNP-UDP domain through an in insert containing inhibitory site. Plant Science, 260, 19-30.
  3. Sharma A, Kumar P, Kesari P, Chaudhary N, Katiki M, Mishra M, Singh PK, Gurjar BR, Sharma AK, Tomar S, Kumar P (2017). Purification and characterization of 2S albumin from seeds of Wrightia tinctoria exhibiting antibacterial and DNase activity. Protein Pept. Lett.,  24 (4), 368-378
  4. Singh A, Kumar N, Tomar PP, Bhose S, Ghosh DK, Roy P, Sharma AK (2017). Characterization of a bacterioferritin comigratory protein family 1-Cys peroxiredoxin from Candidatus Liberibacter asiaticus. Protoplasma, 254(4), 1675-1691.
  5. Kesari P, Neetu, Sharma A, Katiki M, Kumar P, Gurjar BR, Tomar S, Sharma AK, Kumar P (2016). Structural, functional and evolutionary aspects of seed globulins. Protein Pept. Lett., 24 (3), 267-277
  6. Sharma N, Selvakumar P, Saini G, Warghane A, Ghosh DK, Sharma AK. (2016) Crystal structure analysis in Zn2+-bound state and biophysical characterization of CLas-ZnuA2. Biochimica et Biophysica Acta, 1864(12), 1649-1657.
  7. Ghosh DK, Bhose S, Warghane A, Motghare M, Sharma AK, Dhar AK, Gowda S. (2015) Loop-mediated isothermal amplification (LAMP) based method for rapid and sensitive detection of ‘Candidatus Liberibacter asiaticus’  in citrus and the psyllid vector, Diaphornia citri Kuwayama. J. Plant Biochem. Biotechnol. 25 (2), 219-223.
  8. Singh A, Selvakumar P, Saraswat A, Tomar PP, Mishra M, Singh PK, Sharma AK. (2015) Characterization and cloning of an 11S globulin with hemagglutination activity from Murraya paniculata. Protein Pept. Lett., 22(8): 750-761.
  9. Ghosh DK, Bhose S, Motghare M, Warghane A, Mukherjee K, Ghosh DK Sr, Sharma AK, Ladania MS, Gowda S. (2015) Genetic diversity of Indian populations of ‘Candidatus Liberibacter asiaticus’ based on the tandem repeat variability in a genomic locus. Phytopathology, 105(8): 1043-1049.
  10. Kesari P, Patil DN, Kumar P, Tomar S, Sharma AK, Kumar P. (2015) Structural and functional evolution of chitinase-like proteins from plants. Proteomics. 15(10):1693-705. 
  11. Sharma N, Selvakumar P, Bhose S, Ghosh DK, Kumar P, Sharma AK. (2015)  Crystal structure of a periplasmic solute binding protein in metal-free, intermediate and metal-bound states from Candidatus Liberibacter asiaticus. J Struct Biol. 189(3):184-94. 
  12. Tomar PPS, Chaudhary NS, Priyadarshi P, Gahloth D, Patel GK, Selvakumar P, Kumar P and Sharma AK (2014) Purification, characterization and cloning of a 2S albumin with DNase, RNase and antifungal activities from Putranjiva roburghii. Appl Biochem Biotechnol., 174:471-482.
  13. Tomar PPS, Nikhil K, Singh A, Selvakumar P, Roy P and Sharma AK (2014) Characterization of anticancer, DNase and antifungal activity of pumpkin 2S albumin. Biochem. Biophys. Res. Commun., 448; 349-354.
  14. Selvakumar P., Sharma N., Tomar PPS, Kumar P. and Sharma AK (2014). Structural insights into the aggregation behavior of Murraya koenigii miraculin-like protein below pH 7.5. Proteins, 82 (5); 830-840.  DOI: 10.1002/prot.24461
  15. Patel GK, Gupta AK, Gupta A, Mishra M., Singh PK, Saxena AK and Sharma AK. (2014). Purification and physicochemical characterization of a trypsin inhibitor from Cassia Absus Linn. Protein Pept. Lett. 21(2); 108-14.
  16. Patil D.N., Datta M., Dev A., Dhindwal S., Singh N., Dasauni P., Kundu S., Sharma A. K., Tomar S., Kumar P. (2013) Structural investigation of a novel N-acetyl glucosamine binding chi-lectin which reveals evolutionary relationship with class III chitinases. PLoS One 23,8(5), e63779.
  17. Patil D.N., Chaudhary A., Sharma A.K., Tomar S. and Kumar P. (2012) Structural basis for dual inhibitory role of tamarind Kunitz inhibitor (TKI) against factor Xa and trypsin. FEBS J., 279(24); 4547-64, DOI: 10.1111/febs.12042.
  18. Patel G.K., Kawale A.A. and Sharma A. K. (2012). Purification and physicochemical characterization of a serine protease with fibrinolytic activity from latex of medicinal herb Euphorbia hirta. Plant Physiol. Biochem. 52, 104-111.
  19. Patel G.K., Kar B., Sharma A. K. (2012). Characterization of a thermostable family 1 glycosyl hydrolase enzyme from Putranjiva roxburghii seeds. Appl. Biochem. Biotechnol. 166, 523-535. DOI: 10.1007/s12010-011-9445-2.
  20. Pareek N., Vivekanand V., Saroj S., Sharma A. K., Singh R. P. (2012). Purification and characterization of chitin deacetylase from Penicillium oxalicum SAEM-51. Carbohydrate Polymers, 87(2), 1091-1097.
  21. Selvakumar P., Gahloth D., Tomar P.P. S., Sharma N. and Sharma A. K. (2011). Molecular evolution of miraculin-like protein in Kunitz super-family. J. Mol. Evol. 73(5), 369-379
  22. Gahloth D., Shukla U., Birah A., Gupta G.P., Kumar P.A., Dhaliwal H.S. and            Sharma A. K. (2011) Bioinsecticidal activity of Murraya koenigii miraculin-like protein against Helicoverpa armigera and Spodoptera litura. Arch. Insect Biochem and Physiol. 78(3), 132-144.
  23. Patel G.K., Gahloth D., Shee C., Selvakumar P., Sharma A. K. (2011). Stability of Murraya koenigii miraculin-like protein in different physicochemical conditions. Med. Chem. Res. 20, 1542-1549.
  24. Gahloth D., Sharma A. K. (2010). Identification and Partial Characterization of trypsin inhibitory activity in seed of some fruit Plants. J. Plant Biochem. Biotechnol. 19, 235-237.
  25. Gahloth D., Selvakumar P., Shee C., Kumar P., Sharma A. K. (2010) Cloning, sequence analysis and crystal structure determination of a miraculin-like protein from Murraya koenigii. Arch.  Biochem. and Biophys. 494, 15–22.
  26. Tomar S., Patil D.N., Datta M., Tapas S., Preeti, Chaudhary A, Sharma A. K., Tomar S, Kumar P. (2009). Crystallization and preliminary X-ray diffraction analysis of the complex of Kunitz-type tamarind trypsin inhibitor and porcine pancreatic trypsin. Acta Crystallogr Sect F Struct Biol Cryst Commun. 1;65(Pt 11):1179-81.
  27. Patil D.N., Preeti, Chaudhry A., Sharma A. K., Tomar S., Kumar P. (2009) Purification, crystallization and preliminary crystallographic studies of a Kunitz-type proteinase inhibitor from tamarind (Tamarindus indica) seeds. Acta Crystallogr Sect F Struct Biol Cryst Commun. 1;65(Pt 7):736-8.
  28. Patil D. N., Datta M, Chaudhary A, Tomar S, Sharma A. K., Kumar P. (2009) Isolation, purification, crystallization and preliminary crystallographic studies of chitinase from tamarind (Tamarindus indica) seeds. Acta Crystallogr Sect F Struct Biol Cryst Commun. Apr 1; 65(Pt 4):343-5.
  29. Shee C., Agarwal S., Deepankar G., Meena K., Sharma A. K. (2009).Identification of a Peptide-like Compound with Antimicrobial and Trypsin Inhibitory Activity from Seeds of Bottle Gourd (Lagenaria siceraria). J. Plant Biochem. Biotechnol. 18(1), 101-104.
  30. Chaudhary N. S. , Shee C., Islam A, Ahmad F., Yernool D., Kumar P., Sharma A.K., (2008) Purification and characterization of a trypsin inhibitor from Putranjiva roxburghii seeds. Phytochemistry 69, 2120–2126.
  31. Shee C. and Sharma A. K. (2008). Storage and affinity properties of Murraya koenigii  trypsin inhibitor. Food Chem. 107, 312–319.
  32. Shee C., Singh T. P., Kumar P , Sharma A. K. (2007).Crystallization and preliminary X-ray diffraction studies of Murraya koenigii trypsin inhibitor. Acta Crystallograph Sect F   Struct. Biol. Cryst Commun. 1;63 (Pt 4):318-9 
  33. Shee C, Islam A, Ahmad F, Sharma A. K. (2007). Structure–function studies of  Murraya koenigii trypsin inhibitor revealed a stable core beta sheet structure surrounded by α-helices with a possible role for α-helix in inhibitory function. Int. J. Biol. Macromol. 41,410–414.
  34. Shee C. and Sharma A. K. (2007). Purification and characterization of a trypsin inhibitor from the seeds of Murraya koenigii. J. Enz. Inhib. Med. Chem.22,115–120.
  35. Wang B. *, Sharma A.*, Maile R, Saad M., Collins E. J. and Frelinger J. A.(2002). Peptidic termini play a significant role in TCR recognition. J. Immunol. 169, 3137-45

*Both authors contributed equally

41.Kumar S, Sharma A. K., Paramasivam M, Srinivasan A., Singh  T. P. (2001) Three-dimensional structure of a new crystal form of mare lactoferrin in 70% PEG 400 at 3.83A resolution. Indian J Biochem Biophys 38(3), 135-41.

  1. Sharma A. K., Kumar S., Sharma V., Nagpal A., Singh N., Tamboli I., Mani I., Raman, G. and Singh T. P. (2001). Lactoferrin – Melanin interactions and its possible implications in melanin polymerization: crystal structure of the complex formed between mare lactoferrin and melanin monomers at 2.7 A resolution. Proteins 45, 229-236.
  2. Sharma, A. K., Kuhns, J. J., Yan S., Freidline R., Long B., Tisch R. and Collins E. J.(2001). Class I MHC anchor substitutions alter the conformation of T cell receptor contacts. J. Biol. Chem., 276 (24), 21443-21449.
  3. Batalia M. A., Kirksey T. J., Sharma A., Jiang L., Jean-Pierre Abstando, Yan S., Zhao, R., and Collins E. J. (2000) Class I MHC is stabilized against thermal denaturation by physiological concentrations of NaCl. Biochemistry, 39 (30), 9030-9038.
  4. Kumar S, Sharma A. K. and Singh T. P. (2000). Metal substitution in lactoferrins : the crystal structure of  manganese substituted lactoferrin at 3.4 Å resolution. Indian J. Physics (2), 143-146.
  5. Karthikeyan S, Sharma S., Sharma A. K., Yadav S., Paramsivam M., Srinivasn A and Singh T. P. (1999). Structural variability and functional convergence in lactoferrins. Current Science 77 (2), 241-255.
  6. Sharma A. K. and Singh T. P. (1999). Lactoferrin-metal interactions: first crystal structure of a complex of lactoferrin with a lanthanide ion (Sm3+) at 3.4 Å resolution. Acta Cryst D55, 1799-1804.
  7. Sharma A. K. and Singh T. P. (1999). Structure of oxalate-substituted diferric mare lactoferrin at 2.7 Å resolution.  Acta Cryst. D 55, 1792-1798.
  8. Sharma A. K., Rajshankar, K., Yadav M. P. and Singh T. P.(1999). Structure of apo mare lactoferrin: both N and C lobe in closed form. Acta Cryst D 55, 1152-1157.
  9. Sharma A. K., Paramsivam M, Srinivasan A., Yadav M. P. and Singh T. P. (1999). Three-dimensional structure of diferric mare lactoferrin at 2.6 Å resolution. J. Mol.Biol. 289(2), 303-317.
  10. Sharma A. K., Karthikeyan S., Sharma S., Yadav S., Srinivasan A. and Singh T. P. (1998). Structure of buffalo and mare lactoferrin: similarities, differences and flexibility. Adv.Exp. Med. Biol. 443, 15-21.
  11. Kaur P., Sharma A. K., Karthikeyan S., Mitra S. N. and Singh T. P. (1996).  Structure of Mare Lactoferrin at 4A  resolution. Prog. Biophys. Mol. Biol., 65,29.
  12. Sharma A. K., Karthikeyan S., Kaur P., Yadav M. P. and Singh T. P. (1996). Purification, Crystallization and Preliminary Crystallographic Analysis of Mare Lactoferrin. Acta Crystallogr. D. D52, 1196-1198.