Khandekar Jishan Bari

About

My research interests include protein structure determination, conformational dynamics studies and biomolecular interactions to explore the underlying molecular mechanisms using multidimensional high-field NMR spectroscopy. Further, I combine high-resolution NMR studies with a range of low-to-high resolution biophysical tools to arrive at a rigorous understanding of the system in hand. I am also interested in employing molecular dynamics and enhanced sampling techniques to study ligand binding and protein aggregation. With a deep affection in quantum mechanics, I take great interest in the product operator analyses of various pulse sequences extensively used in NMR.

Employment

• The Scripps Research Institute Postdoctoral Associate
  2021 - Present
• Indian Institute of Science Education and Research Berhampur Postdoctoral Fellow
  2020 - 2021
• Tata Institute of Fundamental Research Hyderabad Postdoctoral Research Associate
  2020 - 2020
• Tata Institute of Fundamental Research Hyderabad Ph.D
  2014 - 2020

Education

• Tata Institute of Fundamental Research Hyderabad M.Sc (Integrated M.Sc-Ph.D)
  2014 - 2019
• Jadavpur University B.Sc (Honours)
  2011 - 2014
• The Frank Anthony Public School Higher Secondary (ISC)
  2009 - 2011

Projects & Funding

Projects & funding information is unavailable.

Publications (12)

• Fundamental Challenges and Outlook in Simulating Liquid-Liquid Phase Separation of Intrinsically Disordered Proteins
  Journal of Physical Chemistry Letters 2021 59 citations DOI: 10.1021/acs.jpclett.0c03404
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• The structural biology of crystallin aggregation: challenges and outlook
  FEBS Journal 2021 5 citations DOI: 10.1111/febs.15684
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• A Perspective on Biophysical Studies of Crystallin Aggregation and Implications for Cataract Formation
  Journal of Physical Chemistry B 2020 24 citations DOI: 10.1021/acs.jpcb.0c07449
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• A Molecular Dynamics Perspective To Identify Precursors to Aggregation in Human γS-Crystallin Unravels the Mechanism of Childhood Cataracts.
  The journal of physical chemistry. B 2019 8 citations DOI: 10.1021/acs.jpcb.9b08195
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• Structural studies on the individual domains of human γS-crystallin and its G57W mutant unfolds mechanistic insights into childhood cataracts.
  Biochemical and biophysical research communications 2019 6 citations DOI: 10.1016/j.bbrc.2019.07.094
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• On identifying low energy conformational excited states with differential ruggedness in human γS-crystallin promoting severe infantile cataracts.
  Biochemical and biophysical research communications 2019 6 citations DOI: 10.1016/j.bbrc.2019.05.071
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• Enhanced H/D exchange unravels sequential structural excursions in G57W variant of human γS-crystallin with pro-cataractogenic conformations.
  Biochemical and biophysical research communications 2019 7 citations DOI: 10.1016/j.bbrc.2019.05.029
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• Conformational dynamics study on human γS-crystallin as an efficient route to childhood blindness.
  Biochemical and biophysical research communications 2019 8 citations DOI: 10.1016/j.bbrc.2019.02.124
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• Structure of G57W mutant of human γS-crystallin and its involvement in cataract formation.
  Journal of structural biology 2019 17 citations DOI: 10.1016/j.jsb.2019.02.003
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• Structural and functional characterization of a missense mutant of human γS-crystallin associated with dominant infantile cataracts.
  Biochemical and biophysical research communications 2018 8 citations DOI: 10.1016/j.bbrc.2018.10.187
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• Sequence specific 1H, 13C and 15N resonance assignments of the C-terminal domain of human γS-crystallin.
  Biomolecular NMR assignments 2018 6 citations DOI: 10.1007/s12104-018-9848-x
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• Sequence specific 1H, 13C and 15N resonance assignments of a cataract-related variant G57W of human γS-crystallin.
  Biomolecular NMR assignments 2017 12 citations DOI: 10.1007/s12104-017-9779-y
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