U.S. Department of Health and Human Services
William Eaton

 Contact Info

Tel: 301-496-6030
Email: eaton@helix.nih.gov

 Select Experience

  • Ph.D.University of Pennsylvania1967 M.D.
  • M.D.University of Pennsylvania1964
  • B.A.University of Pennsylvania1959

 Related Links



    William A. Eaton, M.D., Ph.D.

    Chief, Laboratory of Chemical Physics
    NIH Distinguished Investigator, Laboratory of Chemical PhysicsBiophysical Chemistry Section
    • Biomedical Engineering/Biophysics/Physics


    A selection of recent and significant publications can be viewed below.

    Chung HS, McHale K, Louis JM, Eaton WA. Single-molecule fluorescence experiments determine protein folding transition path times. Science. 2012 Feb 24; 335:981-4. [Full Text/Abstract]
    Chung HS, Gopich IV, McHale K, Cellmer T, Louis JM, Eaton WA. Extracting rate coefficients from single-molecule photon trajectories and FRET efficiency histograms for a fast-folding protein. J Phys Chem A. 2011 Apr 28; 115:3642-56. [Full Text/Abstract]
    Cellmer T, Buscaglia M, Henry ER, Hofrichter J, Eaton WA. Making connections between ultrafast protein folding kinetics and molecular dynamics simulations. Proc. Natl. Acad. Sci. U.S.A. 2011 Apr 12; 108:6103-8. [Full Text/Abstract]
    Chung HS, Louis JM, Eaton WA. Experimental determination of upper bound for transition path times in protein folding from single-molecule photon-by-photon trajectories. Proc. Natl. Acad. Sci. U.S.A. 2009 Jul 21; 106:11837-44. [Full Text/Abstract]
    Kubelka J, Henry ER, Cellmer T, Hofrichter J, Eaton WA. Chemical, physical, and theoretical kinetics of an ultrafast folding protein. Proc. Natl. Acad. Sci. U.S.A. 2008 Dec 2; 105:18655-62. [Full Text/Abstract]
    Cellmer T, Henry ER, Hofrichter J, Eaton WA. Measuring internal friction of an ultrafast-folding protein. Proc. Natl. Acad. Sci. U.S.A. 2008 Nov 25; 105:18320-5. [Full Text/Abstract]
    Schuler B, Eaton WA. Protein folding studied by single-molecule FRET. Curr. Opin. Struct. Biol. 2008 Feb; 18:16-26. [Full Text/Abstract]
    Cellmer T, Henry ER, Kubelka J, Hofrichter J, Eaton WA. Relaxation rate for an ultrafast folding protein is independent of chemical denaturant concentration. J. Am. Chem. Soc. 2007 Nov 28; 129:14564-5. [Full Text/Abstract]
    Best RB, Merchant KA, Gopich IV, Schuler B, Bax A, Eaton WA. Effect of flexibility and cis residues in single-molecule FRET studies of polyproline. Proc. Natl. Acad. Sci. U.S.A. 2007 Nov 27; 104:18964-9. [Full Text/Abstract]
    Merchant KA, Best RB, Louis JM, Gopich IV, Eaton WA. Characterizing the unfolded states of proteins using single-molecule FRET spectroscopy and molecular simulations. Proc. Natl. Acad. Sci. U.S.A. 2007 Jan 30; 104:1528-33. [Full Text/Abstract]
    Kubelka J, Chiu TK, Davies DR, Eaton WA, Hofrichter J. Sub-microsecond protein folding. J. Mol. Biol. 2006 Jun 9; 359:546-53. [Full Text/Abstract]
    Christoph GW, Hofrichter J, Eaton WA. Understanding the shape of sickled red cells. Biophys. J. 2005 Feb; 88:1371-6. [Full Text/Abstract]
    Viappiani C, Bettati S, Bruno S, Ronda L, Abbruzzetti S, Mozzarelli A, Eaton WA. New insights into allosteric mechanisms from trapping unstable protein conformations in silica gels. Proc. Natl. Acad. Sci. U.S.A. 2004 Oct 5; 101:14414-9. [Full Text/Abstract]
    Kubelka J, Hofrichter J, Eaton WA. The protein folding 'speed limit'. Curr. Opin. Struct. Biol. 2004 Feb; 14:76-88. [Full Text/Abstract]
    Eaton WA, Henry ER, Hofrichter J, Bettati S, Viappiani C, Mozzarelli A. Evolution of allosteric models for hemoglobin. IUBMB Life. 2007 Aug-Sep; 59:586-99. [Full Text/Abstract]