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Professor; Core Director, Macromolecular Interactions Facility


  • 2014 invited talk, Resources at the Macromolecular Interactions Facility, Structural Biology Symposium at UNC.
  • 2013 invited talk, Resources at the Macromolecular Interactions Facility, Carolina center for Genome Sciences Spring Symposium, “From Genome to Proteome: Proteomic Innovations and Technologies at UNC.
  • 2011, 2009, 2005, 2004 NIH Scientific Review committee member


Dr. Tripathy is the Director of the Macromolecular Interactions Facility, a core facility of the University of North Carolina at Chapel Hill, which provides instrumentation and resources for biophysical characterization of biological macromolecules and their interactions with cognate ligands. Research applications include:

  • Determination of solution molecular weight, oligomeric state and association/dissociation constants of macromolecules
  • Determination of on and off rates (kon and koff), stoichiometry, equilibrium binding constants and other thermodynamic parameters (∆G, ∆H and ∆S) of bimolecular interactions
  • Determination of sedimentation, diffusion and frictional coefficients, hydrodynamic and RMS radius, and second virial coefficient
  • Determinations of secondary structure, melting profile, melting temperature (Tm) and thermal stability

Dr. Tripathy provides training to faculty, post-docs, and students in experimental design, instrument operation, data analysis and interpretation one-on-one basis and through his “Macromolecular Interaction” (BIOC662) course, a critical component of the Biophysics Training Program at UNC and open to all graduate students.


  • A multi-laboratory Comparision of Calibration Accuracy and the Performance of External References in Analytical Ultracentrifugation.120 authors including A. Tripathy. PLOS ONE (in press), 2015.
  • Discovery of a selective, substrate-competitive inhibitor of the lysine methyltransferase SETD8. Ma A, Yu W, Li F, Bleich RM, Herold JM, Butler KV, Norris JL, Korboukh V, Tripathy A, Janzen WP, Arrowsmith CH, Frye SV, Vedadi M, Brown PJ, Jin J.
  • J Med Chem. 2014 Aug 14;57(15):6822-33. doi: 10.1021/jm500871s. Epub 2014 Jul 25
  • The splicing activator DAZAP1 integrates splicing control into MEK/Erk-regulated cell proliferation and migration. Choudhury R, Roy SG, Tsai YS, Tripathy A, Graves LM, Wang Z. Nat Commun. 2014;5:3078. doi: 10.1038/ncomms4078
  • Rajarshi Choudhury, Sreerupa Ghose Roy, Yihsuan S. Tsai, Ashutosh Tripathy, Lee M. Graves and Zefeng Wang. 2014. The splicing activator DAZAP1 integrates splicing
  • control into MEK/Erk-regulated cell proliferation and migration. Nature Communications. 5:3078 | DOI: 10.1038/ncomms4078.
  • Garland, A.L., Walton, W.G., Coakley, R.D., Tan, C.D., Gilmore, R.C., Hobbs, C.A., Tripathy, A., Clunes, L.A., Bencharit, S., Stutts, M.J., Betts, L., Redinbo, M.R., and Tarran, R. 2013. Molecular Basis for pH-Dependent Mucosal Dehydration in Cystic Fibrosis Airways. Proceedings of the National Academy of Sciences USA 110 (40) 15973-15978.
  • Thomas C Freeman, Justin L Black, Holly G Bray, Onur Dagliyan, Yi I. Wu, Ashutosh Tripathy, Nikolay V. Dokholyan, Tina M Leisner, and Leslie V. Parise. (2013). Identification of novel integrin binding partners for CIB1: structural and thermodynamic basis of CIB1 promiscuity. Biochemistry, in press. Publication Date (Web): September 6, 2013 (Article). DOI: 10.1021/bi400678y.
  • Chopra, S., Palencia, A., Virus, C., Tripathy, A., Temple, B.R., Velazquez-Campoy, A., Cusack, S., and Reader, J. S (2013). Plant tumour biocontrol agent employs a tRNA-dependent mechanism to inhibit leucyl-tRNA synthetase . Nature Communications. 4: 1417.
  • Rao L, Romes EM, Nicholas MP, Brenner S, Tripathy A, Gennerich A, Slep KC. 2013.
  • The Yeast Dynein Dyn2-Pac11 Complex is a Dynein Dimerization/Processivity Factor: Structural and Single Molecule Characterization. Mol Biol Cell. 2013 Jun 12. [Epub ahead of print].
  • Cai L, Rothbart SB, Lu R, Xu B, Chen WY, Tripathy A, Rockowitz S, Zheng D, Patel DJ, Allis CD, Strahl BD, Song J, Wang GG. (2013). An H3K36 methylation-engaging Tudor motif of polycomb-like proteins mediates PRC2 complex targeting. Mol Cell. 49(3):571-82. doi: 10.1016/j.molcel.2012.11.026. Epub 2012 Dec 27. PubMed PMID: 23273982; PubMed Central PMCID: PMC3570589

Dr. Ash Tripathy