Carl Frieden, Ph.D.

Carl Frieden

Biochemistry and Molecular Biophysics

Lab Website
Graduate Programs (DBBS)
Publications (PubMed / NIH)

Office: 215 McDonnell Science Building
Phone: 314-362-3344
Email: friedenc(at)


Protein folding, aggregation, intrinsically disordered proteins, fluorescence methods, fluorine NMR

Carl Frieden lab research


  • Wang H., Shu Q., Rempel D.L., Frieden C., and Gross M.L.
    Understanding Curli Amyloid-Protein Aggregation by Hydrogen-Deuterium Exchange and Mass Spectrometry.
    Int J Mass Spectrom. 420:16-23. doi: 10.1016/j.ijms.2016.10.006. (2017) Abstract)

  • Wang H., Rempel D.L., Giblin D., Frieden C., and Gross M.L.
    Peptide-Level Interactions between Proteins and Small-Molecule Drug Candidates by Two Hydrogen-Deuterium Exchange MS-Based Methods: The Example of Apolipoprotein E3.
    Analytical Chem. doi: 10.1021/acs.analchem.7b01121. (2017) (Abstract)

  • Frieden C., Wang H., and Ho C.M.W.
    A mechanism for lipid binding to apoE and the role of intrinsically disordered regions coupled to domain-domain interactions.
    Proc Natl Acad Sci U S A. 114(24):6292-6297. (2017) (Abstract)

  • Wang H., Shu Q., Frieden C., and Gross M.L.
    Deamidation slows Curli Amyloid-Protein Aggregation.
    Biochemistry. (2017) (Abstract)

  • Shu, Q., Krezel, A.M., Cusumano, Z.T., Pinkner, J.S., Klein, R., Hultgren, S.J. and Frieden, C.
    Solution NMR structure of CsgE: Structural insights into a chaperone and regulator protein important for functional amyloid formation.
    Proc Natl Acad Sci USA 113:7130-7135 (2016) (Abstract)

  • Mondal, T., Wang, H., DeKoster, G.T., Baban, B., Gross, M.L. and Frieden, C.
    ApoE: In Vitro Studies of a Small Molecule Effector.
    Biochemistry 55:2613-2621 (2016). (Abstract)

  • Wang, H., Shu, Q., Rempel, D.L., Frieden, C. and Gross, M.L.
    Continuous and pulsed hydrogen-deuterium exchange and mass spectrometry characterize CsgE oligomerization.
    Biochemistry 54:6475-6481 (2015). (Abstract)

  • Frieden, C.
    ApoE: the role of conserved residues in defining function.
    Protein Sci 24:138-144 (2015). (Abstract)

  • Garai, K., Verghese, P.B., Baban, B., Holtzman, D.M. and Frieden, C.
    The binding of apolipoprotein E to oligomers and fibrils of amyloid-β alters the kinetics of amyloid aggregation.
    Biochemistry 53:6323-6331 (2014). (Abstract)

  • Hammes, G. and Frieden, C.
    Robert A. Alberty“.
    Biographical Memoirs Natl Acad of Sci. (2014). (Abstract)