TIFR
Department of Chemical Sciences
School of Natural Sciences

K. V. R. Chary

K. V. R. Chary
Senior Professor
Department of Chemical Sciences
Office
:
NMR-202, Department of Chemical Sciences
Tata Institute of Fundamental Research
Homi Bhabha Road, Colaba
Mumbai, 400 005, India
Phone
:
91 22 2278 2489
91 22 2278 3489 (Res)
91 22 2280 4860 (Res)
Mobile
:
9987260959
Fax
:
91 22 2280 4610
Email
:
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Academic Profile
Doctoral Degree
:
1983, Osmania University, Hyderabad, Andhra Pradesh, India.
Postdoctoral Experience
:
1988-1990, ETH Zurich Switzerland.
  • Current Research
  • Selected Publications

Investigation of the 3D structures and properties of biological molecules, particularly proteins and nucleic acids, in atomic detail and their correlation with biological activity; Protein Engineering; Development of NMR methodologies and algorithms for NMR assignments and 3D structural analysis.

  • R. P. Barnwal, M. K. Jobby, K. M. Devi, Y. Sharma, K. V. R. Chary,* Solution structure and calcium-binding properties of M-crystallin, a primordial βϒ-crystallin from archaea. (2009), J. Mol. Biology, 386, 675-689.
  • S. M. Mustafi, R. B. Mutalik, R. Jain, K. Chandra, A. Bhattacharya and K. V. R. Chary,* Structural characterization of a novel Ca2+-binding protein from Entamoeba histolytica: Structural basis for the observed functional differences with its isoform. (2009), J. Bio. Inorg. Chem., 14, 471-483.
  • Aravind P, Chandra K, Reddy PP, Jeromin A, Chary KVR* and Sharma Y (2008) Regulatory and structural EF-hand motifs of neuronal calcium sensor-1: Mg2+ modulates Ca2+-binding, Ca2+-induced conformational dynamics and equilibrium unfolding transitions, J. Mol. Biology 376 1100-15.
  • Barnwal RP, Atreya HS*, Chary KVR* (2008) Chemical shift based editing of CH3 groups in fractionally 13C-labelled proteins using GFT (3, 2)D CT-HCCH-COSY: stereospecific assignments of CH3 groups of Val and Leu residues., J Biomol NMR 42 149-54.
  • Barnwal RP, Ashok K. Rout, H. S. Atrya, Chary KVR* (2008) Identification of C-terminal neighbours of amino acid residues without an aliphatic 13Cϒ as an aid to NMR assignments in proteins. J Biomol NMR 4 191-7.
  • Barnwal RP, Rout AK, Chary KVR* and Atreya HS, (2008) Rapid Measurement of pseudocontact shifts in paramagentic proteins by GFT NMR spectroscopy., The Open Magnetic Resonance Journal 1 16-28.
  • Rapid measurement of 3J(HN-Hα) and 3J(N-Hβ) coupling constants in polypeptides. (2007), R. P. Barnwal, Ashok K. Rout, K. V. R. Chary* and H. S. Atreya, J. Biomol. NMR, 39(4), 259-63.
  • S. M. Mustafi, S. Mukherjee, K. V. R. Chary*, Cristina Del Bianco and Claudio Luchinat (2004) Energetics and mechanism of Ca2+ displacement by lanthanides in a calcium binding protein., Biochemistry, 43, 9320-9331.
  • Rani Parvathy.V., Sukesh R. Bhaumik, K. V. R. Chary*, G. Govil, Keliang Liu, Frank B. Howard and H. Todd Miles, NMR Structure of a parallel stranded DNA duplex at atomic resolution. (2002), Nucleic Acids Res., 30, 1500-1511
  • H.S. Atreya, S. C. Sahu, A. Bhattacharya, K. V. R. Chary* and G. Govil, NMR derived solution structure of an EF-hand Calcium binding protein from Entamoeba histolytica. (2001), Biochemistry 40, 14392-14403.
  • H. S. Atreya and K. V. R. Chary,* Selective ‘unlabeling’ of amino acids in fractionally 13C labeled proteins: An approach for stereospecific NMR assignments of CH3 groups in Val and Leu residues. (2001), J. Biomol. NMR., 19, 267-272.
  • H. S. Atreya, S. C. Sahu, K. V. R. Chary,* and G. Govil, A Tracked AuTomated Assignments in PROteins (TATAPRO). (2000), J. Biomol. NMR., 17, 125-136.
  • Mahua Ghosh, N. Vinay Kumar, Umesh Varshney and K. V. R. Chary*, Structural basis for Uracil DNA glycosylase interaction with uracil: NMR study. (2000), Nucleic Acids Res., 28, 1906-1912.
  • S. C. Sahu, A. Bhattacharya, K. V. R. Chary,* and G. Govil, Secondary structure of a calcium binding protein (CaBP) from Entamoeba histolytic. (1999), FEBS Letters., 459, 51-56.
  • Karthikeyan G, K. V. R. Chary* and Basuthkar J Rao, Fold-back structures at distal end influence DNA slippage at proximal end during mononucleotide repeat expansions. (1999), Nucleic Acids Res., 27, 3851-3858.
  • S. R. Baumik, K. V. R. Chary*, G. Govil, L. Keliang, and H.T. Miles, NMR characterization of a triple-stranded complex formed by homo-purine and homo-pyrimidine DNA strands at 1:1 molar ratio and acidic pH. (1995), Nucleic Acids Res., 23, 4116-4121.
  • K. V. R. Chary*, V.K. Rastogi, & G. Govil, An Efficient 2D NMR Technique HELCO for Heteronuclear [31P-1H] Longrange Correlation. (1993), J. Magn. Reson., B 102, 81-83.
  • K. V. R. Chary*, G. Otting and K. Wuthrich, Mesurement of small heteronuclear 1H-15N coupling constants in 15N labelled proteins by 3D HNNHAB–COSY. (1991), J. Magn. Reson., 93, 218-224.
  • K. V. R. Chary* and Sandeep Modi, Analysis of intrasugar interproton NOESY cross-peaks as an aid to determine sugar geometries in DNA fragments. (1988), FEBS Lett., 233, 319-325.
  • K. V. R. Chary*, R.V. Hosur, Tan zu-kun, G. Govil and H.T. Miles, Novel solution conformation of DNA observed in d-GAATTCGAATTC by 2D NMR. (1987), Biochemistry, 26, 1315-1322.