Hoi Sung Chung, Ph.D.

Photo of Hoi Sung Chung
Scientific Focus Areas: Biomedical Engineering and Biophysics, Structural Biology

Publications

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

Select Publications

Transition Path Times Measured by Single-Molecule Spectroscopy.
Chung HS.
J Mol Biol (2018 Feb 16) 430:409-423. Abstract/Full Text
Oligomerization of the tetramerization domain of p53 probed by two- and three-color single-molecule FRET.
Chung HS, Meng F, Kim JY, McHale K, Gopich IV, Louis JM.
Proc Natl Acad Sci U S A (2017 Aug 15) 114:E6812-E6821. Abstract/Full Text
Analysis of Fluorescence Lifetime and Energy Transfer Efficiency in Single-Molecule Photon Trajectories of Fast-Folding Proteins.
Chung HS, Louis JM, Gopich IV.
J Phys Chem B (2016 Feb 4) 120:680-99. Abstract/Full Text

Additional Publications

Probing the mechanism of inhibition of amyloid-β(1-42)-induced neurotoxicity by the chaperonin GroEL.
Wälti MA, Steiner J, Meng F, Chung HS, Louis JM, Ghirlando R, Tugarinov V, Nath A, Clore GM.
Proc Natl Acad Sci U S A (2018 Dec 18) 115:E11924-E11932. Abstract/Full Text
Diffusion-limited association of disordered protein by non-native electrostatic interactions.
Kim JY, Meng F, Yoo J, Chung HS.
Nat Commun (2018 Nov 9) 9:4707. Abstract/Full Text
Three-Color Single-Molecule FRET and Fluorescence Lifetime Analysis of Fast Protein Folding.
Yoo J, Louis JM, Gopich IV, Chung HS.
J Phys Chem B (2018 Oct 10) Abstract/Full Text
Highly Disordered Amyloid-β Monomer Probed by Single-Molecule FRET and MD Simulation.
Meng F, Bellaiche MMJ, Kim JY, Zerze GH, Best RB, Chung HS.
Biophys J (2018 Feb 27) 114:870-884. Abstract/Full Text
Protein folding transition path times from single molecule FRET.
Chung HS, Eaton WA.
Curr Opin Struct Biol (2018 Feb) 48:30-39. Abstract/Full Text
Structural origin of slow diffusion in protein folding.
Chung HS, Piana-Agostinetti S, Shaw DE, Eaton WA.
Science (2015 Sep 25) 349:1504-10. Abstract/Full Text
Testing Landscape Theory for Biomolecular Processes with Single Molecule Fluorescence Spectroscopy.
Truex K, Chung HS, Louis JM, Eaton WA.
Phys Rev Lett (2015 Jul 3) 115:018101. Abstract/Full Text
Fast single-molecule FRET spectroscopy: theory and experiment.
Chung HS, Gopich IV.
Phys Chem Chem Phys (2014 Sep 21) 16:18644-57. Abstract/Full Text
Single-molecule fluorescence probes dynamics of barrier crossing.
Chung HS, Eaton WA.
Nature (2013 Oct 31) 502:685-8. Abstract/Full Text
Measuring ultrafast protein folding rates from photon-by-photon analysis of single molecule fluorescence trajectories.
Chung HS, Cellmer T, Louis JM, Eaton WA.
Chem Phys (2013 Aug 30) 422:229-237. Abstract/Full Text
Solution structure of the ESCRT-I and -II supercomplex: implications for membrane budding and scission.
Boura E, Różycki B, Chung HS, Herrick DZ, Canagarajah B, Cafiso DS, Eaton WA, Hummer G, Hurley JH.
Structure (2012 May 9) 20:874-86. Abstract/Full Text
Single-molecule fluorescence experiments determine protein folding transition path times.
Chung HS, McHale K, Louis JM, Eaton WA.
Science (2012 Feb 24) 335:981-4. Abstract/Full Text
Solution structure of the ESCRT-I complex by small-angle X-ray scattering, EPR, and FRET spectroscopy.
Boura E, Rózycki B, Herrick DZ, Chung HS, Vecer J, Eaton WA, Cafiso DS, Hummer G, Hurley JH.
Proc Natl Acad Sci U S A (2011 Jun 7) 108:9437-42. Abstract/Full Text
Extracting rate coefficients from single-molecule photon trajectories and FRET efficiency histograms for a fast-folding protein.
Chung HS, Gopich IV, McHale K, Cellmer T, Louis JM, Eaton WA.
J Phys Chem A (2011 Apr 28) 115:3642-56. Abstract/Full Text
Distinguishing between protein dynamics and dye photophysics in single-molecule FRET experiments.
Chung HS, Louis JM, Eaton WA.
Biophys J (2010 Feb 17) 98:696-706. Abstract/Full Text
Experimental determination of upper bound for transition path times in protein folding from single-molecule photon-by-photon trajectories.
Chung HS, Louis JM, Eaton WA.
Proc Natl Acad Sci U S A (2009 Jul 21) 106:11837-44. Abstract/Full Text
Probing the folding transition state of ubiquitin mutants by temperature-jump-induced downhill unfolding.
Chung HS, Shandiz A, Sosnick TR, Tokmakoff A.
Biochemistry (2008 Dec 30) 47:13870-7. Abstract/Full Text
Temperature-dependent downhill unfolding of ubiquitin. II. Modeling the free energy surface.
Chung HS, Tokmakoff A.
Proteins (2008 Jul) 72:488-97. Abstract/Full Text
Temperature-dependent downhill unfolding of ubiquitin. I. Nanosecond-to-millisecond resolved nonlinear infrared spectroscopy.
Chung HS, Tokmakoff A.
Proteins (2008 Jul) 72:474-87. Abstract/Full Text
Amide I two-dimensional infrared spectroscopy of proteins.
Ganim Z, Chung HS, Smith AW, Deflores LP, Jones KC, Tokmakoff A.
Acc Chem Res (2008 Mar) 41:432-41. Abstract/Full Text
Transient 2D IR spectroscopy of ubiquitin unfolding dynamics.
Chung HS, Ganim Z, Jones KC, Tokmakoff A.
Proc Natl Acad Sci U S A (2007 Sep 4) 104:14237-42. Abstract/Full Text
Transient two-dimensional IR spectrometer for probing nanosecond temperature-jump kinetics.
Chung HS, Khalil M, Smith AW, Tokmakoff A.
Rev Sci Instrum (2007 Jun) 78:063101. Abstract/Full Text
The anharmonic vibrational potential and relaxation pathways of the amide I and II modes of N-methylacetamide.
DeFlores LP, Ganim Z, Ackley SF, Chung HS, Tokmakoff A.
J Phys Chem B (2006 Sep 28) 110:18973-80. Abstract/Full Text
Visualization and characterization of the infrared active amide I vibrations of proteins.
Chung HS, Tokmakoff A.
J Phys Chem B (2006 Feb 16) 110:2888-98. Abstract/Full Text
Residual native structure in a thermally denatured beta-hairpin.
Smith AW, Chung HS, Ganim Z, Tokmakoff A.
J Phys Chem B (2005 Sep 15) 109:17025-7. Abstract/Full Text
Conformational changes during the nanosecond-to-millisecond unfolding of ubiquitin.
Chung HS, Khalil M, Smith AW, Ganim Z, Tokmakoff A.
Proc Natl Acad Sci U S A (2005 Jan 18) 102:612-7. Abstract/Full Text
Two-dimensional infrared spectroscopy of antiparallel beta-sheet secondary structure.
Demirdöven N, Cheatum CM, Chung HS, Khalil M, Knoester J, Tokmakoff A.
J Am Chem Soc (2004 Jun 30) 126:7981-90. Abstract/Full Text