Jonathan A. King

Jonathan A. King

Professor Emeritus

Jonathan A. King studies what happens when proteins do not fold properly — leading to conditions like cataracts — and works to protect the conditions needed to support biomedical research.



Cindy Woolley



Assistant Phone


PhD 1968, California Institute of Technology

Research Summary

After decades of investigating protein folding, misfolding and aggregation, and bacteriophage structure and assembly, I am now concentrating on protecting the conditions needed to support biomedical research, in particular federal investment in biomedical research through the NIH and NSF budgets. This involves not only advocating for these investments, but critiquing the critiquing the enormous drain on productive investment of our tax dollars through excessive military spending, particularly on nuclear weapons. To this end I chair the Reducing the Threat of Nuclear War Conference held annually in the Spring at MIT, and chair the Nuclear Disarmament Working Group of Mass Peace Action which provides national leadership on nuclear disarmament. Jonathan King is no longer accepting students.


  • NIH MERIT Award
  • Guggenheim Fellow
  • Jane Coffin Childs Fellow
  • MIT MLK Jr Faculty Leadership

Recent Publications

  1. Aggregation of Trp > Glu point mutants of human gamma-D crystallin provides a model for hereditary or UV-induced cataract. Serebryany, E, Takata, T, Erickson, E, Schafheimer, N, Wang, Y, King, JA. 2016. Protein Sci. 25, 1115-28.
    doi: 10.1002/pro.2924PMID:26991007
  2. Copper and Zinc Ions Specifically Promote Nonamyloid Aggregation of the Highly Stable Human γ-D Crystallin. Quintanar, L, Domínguez-Calva, JA, Serebryany, E, Rivillas-Acevedo, L, Haase-Pettingell, C, Amero, C, King, JA. 2016. ACS Chem. Biol. 11, 263-72.
    doi: 10.1021/acschembio.5b00919PMID:26579725
  3. Wild-type human γD-crystallin promotes aggregation of its oxidation-mimicking, misfolding-prone W42Q mutant. Serebryany, E, King, JA. 2015. J. Biol. Chem. 290, 11491-503.
    doi: 10.1074/jbc.M114.621581PMID:25787081
  4. Biochemical characterization of mutants in chaperonin proteins CCT4 and CCT5 associated with hereditary sensory neuropathy. Sergeeva, OA, Tran, MT, Haase-Pettingell, C, King, JA. 2014. J. Biol. Chem. 289, 27470-80.
    doi: 10.1074/jbc.M114.576033PMID:25124038
  5. The βγ-crystallins: native state stability and pathways to aggregation. Serebryany, E, King, JA. 2014. Prog. Biophys. Mol. Biol. 115, 32-41.
    doi: 10.1016/j.pbiomolbio.2014.05.002PMID:24835736
  6. Human CCT4 and CCT5 chaperonin subunits expressed in Escherichia coli form biologically active homo-oligomers. Sergeeva, OA, Chen, B, Haase-Pettingell, C, Ludtke, SJ, Chiu, W, King, JA. 2013. J. Biol. Chem. 288, 17734-44.
    doi: 10.1074/jbc.M112.443929PMID:23612981
  7. Human TRiC complex purified from HeLa cells contains all eight CCT subunits and is active in vitro. Knee, KM, Sergeeva, OA, King, JA. 2013. Cell Stress Chaperones 18, 137-44.
    doi: 10.1007/s12192-012-0357-zPMID:23011926
  8. Cataract-causing defect of a mutant γ-crystallin proceeds through an aggregation pathway which bypasses recognition by the α-crystallin chaperone. Moreau, KL, King, JA. 2012. PLoS ONE 7, e37256.
    doi: 10.1371/journal.pone.0037256PMID:22655036
  9. Protein misfolding and aggregation in cataract disease and prospects for prevention. Moreau, KL, King, JA. 2012. Trends Mol Med 18, 273-82.
    doi: 10.1016/j.molmed.2012.03.005PMID:22520268
  10. Inhibition of unfolding and aggregation of lens protein human gamma D crystallin by sodium citrate. Goulet, DR, Knee, KM, King, JA. 2011. Exp. Eye Res. 93, 371-81.
    doi: 10.1016/j.exer.2011.04.011PMID:21600897
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