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    Last Name

    Sagar V Kathuria PhD

    InstitutionUniversity of Massachusetts Medical School
    DepartmentBiochemistry and Molecular Pharmacology
    AddressUniversity of Massachusetts Medical School
    55 Lake Ave North
    Worcester MA 01605
      Other Positions
      InstitutionUMMS - Graduate School of Biomedical Sciences
      DepartmentBiochemistry and Molecular Pharmacology


        Sequence determinants of protein folding mechanisms: structure of the unfolded state, early events in folding, structures of folding intermediates and stability of the native state.

        The role of Branched Aliphatic Side Chains (BASiC) in defining the folding free energy landscape of globular proteins.

        Cluster analysis of hydrophobic contacts in protein structures - website

        Profiles on Researcher IDGoogle ScholarFaculty of 1000Academia.eduLinkedin, ResearchGate.

        selected publications
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        1. Kathuria SV, Chan YH, Nobrega RP, Özen A, Matthews CR. Clusters of isoleucine, leucine, and valine side chains define cores of stability in high-energy states of globular proteins: Sequence determinants of structure and stability. Protein Sci. 2016 Mar; 25(3):662-75.
          View in: PubMed
        2. Orevi T, Rahamim G, Amir D, Kathuria S, Bilsel O, Matthews CR, Haas E. Sequential Closure of Loop Structures Forms the Folding Nucleus during the Refolding Transition of the Escherichia coli Adenylate Kinase Molecule. Biochemistry. 2016 Jan 12; 55(1):79-91.
          View in: PubMed
        3. Rosen LE, Kathuria SV, Matthews CR, Bilsel O, Marqusee S. Non-native structure appears in microseconds during the folding of E. coli RNase H. J Mol Biol. 2015 Jan 30; 427(2):443-53.
          View in: PubMed
        4. Nobrega RP, Arora K, Kathuria SV, Graceffa R, Barrea RA, Guo L, Chakravarthy S, Bilsel O, Irving TC, Brooks CL, Matthews CR. Modulation of frustration in folding by sequence permutation. Proc Natl Acad Sci U S A. 2014 Jul 22; 111(29):10562-7.
          View in: PubMed
        5. Kathuria SV, Kayatekin C, Barrea R, Kondrashkina E, Graceffa R, Guo L, Nobrega RP, Chakravarthy S, Matthews CR, Irving TC, Bilsel O. Microsecond barrier-limited chain collapse observed by time-resolved FRET and SAXS. J Mol Biol. 2014 May 1; 426(9):1980-94.
          View in: PubMed
        6. Kathuria SV, Chan A, Graceffa R, Paul Nobrega R, Robert Matthews C, Irving TC, Perot B, Bilsel O. Advances in turbulent mixing techniques to study microsecond protein folding reactions. Biopolymers. 2013 Nov; 99(11):888-96.
          View in: PubMed
        7. Graceffa R, Nobrega RP, Barrea RA, Kathuria SV, Chakravarthy S, Bilsel O, Irving TC. Sub-millisecond time-resolved SAXS using a continuous-flow mixer and X-ray microbeam. J Synchrotron Radiat. 2013 Nov; 20(Pt 6):820-5.
          View in: PubMed
        8. Gangadhara BN, Laine JM, Kathuria SV, Massi F, Matthews CR. Clusters of branched aliphatic side chains serve as cores of stability in the native state of the HisF TIM barrel protein. J Mol Biol. 2013 Mar 25; 425(6):1065-81.
          View in: PubMed
        9. Kathuria SV, Guo L, Graceffa R, Barrea R, Nobrega RP, Matthews CR, Irving TC, Bilsel O. Minireview: structural insights into early folding events using continuous-flow time-resolved small-angle X-ray scattering. Biopolymers. 2011 Aug; 95(8):550-8.
          View in: PubMed
        10. Hills RD, Kathuria SV, Wallace LA, Day IJ, Brooks CL, Matthews CR. Topological frustration in beta alpha-repeat proteins: sequence diversity modulates the conserved folding mechanisms of alpha/beta/alpha sandwich proteins. J Mol Biol. 2010 Apr 30; 398(2):332-50.
          View in: PubMed
        11. Yang X, Kathuria SV, Vadrevu R, Matthews CR. Betaalpha-hairpin clamps brace betaalphabeta modules and can make substantive contributions to the stability of TIM barrel proteins. PLoS One. 2009; 4(9):e7179.
          View in: PubMed
        12. Kathuria SV, Day IJ, Wallace LA, Matthews CR. Kinetic traps in the folding of beta alpha-repeat proteins: CheY initially misfolds before accessing the native conformation. J Mol Biol. 2008 Oct 3; 382(2):467-84.
          View in: PubMed
        13. Wu Y, Vadrevu R, Kathuria S, Yang X, Matthews CR. A tightly packed hydrophobic cluster directs the formation of an off-pathway sub-millisecond folding intermediate in the alpha subunit of tryptophan synthase, a TIM barrel protein. J Mol Biol. 2007 Mar 9; 366(5):1624-38.
          View in: PubMed
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