Santosh Kumar Jha

Santosh Kumar Jha

Physical and Materials Chemistry Division

Professional Experience

Jan 2023 – Present: Senior Principal Scientist, CSIR-National Chemical Laboratory, Pune, India

Jan 2018 – Jan 2023: Principal Scientist, CSIR-National Chemical Laboratory, Pune, India

Jan 2014 – Jan 2018: Senior Scientist, CSIR-National Chemical Laboratory, Pune, India

Apr 2012 – Jan 2014:  Postdoctoral Scholar, University of California, Berkeley, USA (Advisor: Prof. Susan Marqusee)

Feb 2010 - Mar 2012: Postdoctoral Scholar, Stanford University, Stanford, USA (Advisor: Prof. Steven G. Boxer)

Oct 2003 - Nov 2009:  Ph.D., National Centre for Biological Sciences, TIFR, Bangalore, India (Advisor: Prof. Jayant B. Udgaonkar)

Selected Publications

  • Pillai M and Jha SK, Conformational Enigma of TDP-43 Misfolding in Neurodegenerative Disorders, ACS Omega., 9, 40286 - 40297 (2024), DOI:doi.org/10.1021/acsomega.4c04119.
  • Patni D, Patil AD, Kirmire MS And Jha A and Jha SK, DNA-mediated formation of phase-separated coacervates of the nucleic acid-binding domain of TAR DNA binding protein (TDP-43) prevents its amyloid-like misfolding, ACS Chem. Neurosci., 15, 4105 - 4122 (2024), DOI:10.1021/acschemneuro.4c00117.
  • Doke AA and Jha SK, Identification of a Hidden, Highly Aggregation-prone Intermediate of Full-length TDP-43 that Triggers its Misfolding and Amyloid Aggregation, Biochemistry., 63, 63, 3100?3 - 3113 (2024), DOI:10.1021/acs.biochem.4c00389.
  • Pillai M, Patil AD And Das A and Jha SK, Pathological mutations D169G and P112H electrostatically aggravate the amyloidogenicity of the functional domain of TDP-43, ACS Chem. Neurosci., 15, 4267 - 4283 (2024), DOI:10.1021/acschemneuro.4c00372.
  • Tamara V, Doke AA And Jha SK and Das A, Deciphering the Monomeric and Dimeric Conformational Landscapes of the Full-length TDP-43 and the Impact of the C-terminal Domain, ACS Chem. Neurosci., 15, 4305 - 4321 (2024), DOI:10.1021/acschemneuro.4c00557.
  • More SR and Jha SK, Multi-Site Red-Edge Excitation Shift Reveals the Residue-Specific Solvation Dynamics During the Native to Amyloid-like Transition of an Amyloidogenic Protein, J. Phys. Chem. B., IN PRESS, (2024).
  • Pillai M And Das A And Jha SK, Electrostatic modulation of intramolecular and intermolecular interactions during the formation of an amyloid-like assembly, Biochemistry., 62, 1890 - 1905 (2023), DOI:10.1021/acs.biochem.3c00014.
  • Pillai M And Jha SK, Multi-step molecular mechanism of amyloid-like aggregation of nucleic acid-binding domain of TDP-43, Proteins: Struct. Funct. Genet., 91, 649 - 664 (2023), DOI:10.1002/prot.26455.
  • Doke AA And Jha SK, Effect of in-vitro solvation condition on inter and intra-molecular assembly of full-length TDP-43, J. Phys. Chem. B., 126, 4799 - 4813 (2022).
  • Mishra P, Patni D And Jha SK, A pH-dependent protein stability switch coupled to the perturbed pKa of a single ionizable residue, Biophys. Chem., 274, 106591 (2021).
  • Patni D And Jha SK, Protonation-deprotonation switch controls the amyloid-like misfolding of nucleic acid binding domains of TDP-43, J. Phys. Chem. B., 125, 30, 8383 - 8394 (2021).
  • Mishra P And Jha SK, Slow motion protein dance visualized using red edge excitation shift of a buried fluorophore, J. Phys. Chem. B., 123, 1256 - 1264 (2019).
  • Pillai M And Jha SK, The folding and aggregation energy landscapes of tethered RRM domains of human TDP-43 are coupled via a metastable molten globule-like oligomer, Biochemistry., 58, 608 - 620 (2019).
  • Mishra P And Jha SK, An alternatively packed dry molten globule-like intermediate in the native state ensemble of a multi-domain protein, J. Phys. Chem. B., 121, 9336 - 9347 (2017).
  • Acharya N, Mishra P And Jha SK, A dry molten globule-like intermediate during the base-induced unfolding of a multidomain protein, Phys. Chem. Chem. Phys., 19, 30207 - 30216 (2017).
  • Acharya N, Mishra P And Jha SK, Evidence for dry molten globule-like domains in the pH-induced equilibrium folding intermediate of a multi-domain protein, J. Phys. Chem. Lett., 7, 173 - 179 (2016).
  • Jha SK And Marqusee S, Kinetic evidence for a two-stage mechanism of protein denaturation by guanidinium chloride, Proc. Natl. Acad. Sci. USA., 111, 4856 - 4861 (2014).
    Recommended by Faculty of 1000 Biology http://f1000.com/prime/718313266
  • Jha SK, Ji M, Gaffney KJ And Boxer SG, Direct measurement of the protein response to an electrostatic perturbation that mimics the catalytic cycle in ketosteroid isomerase, Proc. Natl. Acad. Sci. USA., 108, 16612 - 16617 (2011).
  • Jha SK And Udgaonkar JB, Direct evidence for a dry molten globule intermediate during the unfolding of a small protein, Proc. Natl. Acad. Sci. USA., 106, 12289 - 12294 (2009), DOI:(Recommended by Faculty of 1000 Biology http://f1000.com/14021991).
    Recommended by Faculty of 1000 Biology http://f1000.com/14021991
  • Jha SK, Dhar D, Krishnamoorthy G And Udgaonkar JB , Continuous dissolution of structure during the unfolding of a small protein, Proc. Natl. Acad. Sci. USA., 106, 11113 - 11118 (2009).
  • Jha SK And Udgaonkar JB , Exploring the cooperativity of the fast folding reaction of a small protein using pulsed thiol labeling and mass spectrometry, J. Biol. Chem., 282, 37479 - 37491 (2007).

Research Interest

  • Structural Biology
  • Chemical Biology
  • Physical Chemistry
  • Laser spectroscopy & Instrumentation
  • Spectroscopy
  • Human Diseases
  • Kinetics analysis of Chemical Reactions
  • Protein Chemistry and Proteomics
  • Biological Mass Spectrometry
  • Biophysical Science

Contact Details

Dr. Santosh Kumar Jha
Senior Principal Scientist
Physical and Materials Chemistry Division
Office: F - 101, Polymer and Advanced Materials Laboratory
CSIR - National Chemical Laboratory
Dr. Homi Bhabha Road
Pune 411008, India

Phone: +91-20-25902588
Fax: +91-20-25902615
E-mail: sk.jha@ncl.res.in