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Daniel Jacobson

Daniel Jacobson

· Bruce D. Benson Professor of Philosophy

University of Colorado Boulder · Philosophy

Active 2011–2024

h-index11
Citations721
Papers269 last 5y
Funding
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About

Daniel Jacobson is the Bruce D. Benson Professor of Philosophy at the University of Colorado Boulder. His work encompasses a range of topics in ethics, moral psychology, aesthetics, and the moral and political philosophy of J. S. Mill. He has published extensively on issues concerning sentimentalism, the philosophy of emotion, and freedom of speech. Jacobson was the Project Leader of The Science of Ethics, a three-year project funded by the John Templeton Foundation, and has held fellowships from notable institutions including the National Endowment for the Humanities, the American Council of Learned Societies, the Institute for Humane Studies, the Murphy Institute at Tulane University, and the Princeton University Center for Human Values. His contributions to aesthetics have been recognized with the John Fisher Memorial Prize, and his work has been broadly reprinted and translated into several languages. Jacobson has also co-edited a volume on moral psychology and human agency and is working on a forthcoming book titled 'Solving the Mill Problem: How to Reconcile the Principles of Liberty and Utility.'

Research topics

  • Crystallography
  • Chemistry
  • Quantum mechanics
  • Biology
  • Biochemistry
  • Chemical physics
  • Physics
  • Thermodynamics
  • Biophysics

Selected publications

  • Free-energy changes of bacteriorhodopsin point mutants measured by single-molecule force spectroscopy

    Proceedings of the National Academy of Sciences · 2021 · 20 citations

    1st authorCorresponding
    • Chemistry
    • Crystallography
    • Biophysics

    for a fully folded membrane protein embedded in its native bilayer.

  • Quantifying the Native Energetics Stabilizing Bacteriorhodopsin by Single-Molecule Force Spectroscopy

    Physical Review Letters · 2020 · 22 citations

    • Crystallography
    • Chemical physics
    • Physics

    We quantified the equilibrium (un)folding free energy ΔG_{0} of an eight-amino-acid region starting from the fully folded state of the model membrane-protein bacteriorhodopsin using single-molecule force spectroscopy. Analysis of equilibrium and nonequilibrium data yielded consistent, high-precision determinations of ΔG_{0} via multiple techniques (force-dependent kinetics, Crooks fluctuation theorem, and inverse Boltzmann analysis). We also deduced the full 1D projection of the free-energy landscape in this region. Importantly, ΔG_{0} was determined in bacteriorhodopsin's native bilayer, an advance over traditional results obtained by chemical denaturation in nonphysiological detergent micelles.

Frequent coauthors

  • Thomas T. Perkins

    National Institute of Standards and Technology

    20 shared
  • Omar A. Saleh

    University of California, Santa Barbara

    11 shared
  • Mark J. Stevens

    Sandia National Laboratories

    5 shared
  • Dustin B. McIntosh

    University of California, Santa Barbara

    4 shared
  • Eric R. Switzer

    4 shared
  • Lyle Uyetake

    National Institute of Standards and Technology

    4 shared
  • Yen‐Ting Lin

    4 shared
  • Amir Hajian

    3 shared

Education

  • B.A.

    Yale

  • Ph.D.

    Michigan

Awards & honors

  • John Fisher Memorial Prize

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