Carl Frieden

Carl Frieden

Carl Frieden, Ph.D.

Biochemistry and Molecular Biophysics

Lab Website
Research Opportunities


Office: 215 McDonnell Science Building
Phone: 314-362-3344
Email: frieden at


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

Carl Frieden lab research

Most Recent Publications

  • 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 apoE to oligomers and fibrils of amyloid-beta 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]
  • Crick, S.L., Ruff, K.M., Garai, K., Frieden, C. and Pappu, R.V. Unmasking the Roles of N- and C-terminal Flanking Sequences from Exon 1 of Huntingtin as Modulators of Polyglutamine Aggregation. PNAS 110:20075-20080 (2013). [Abstract]
  • Frieden, C. and Garai, K. Concerning the structure of apoE. Protein Sci. 22:1820-1825 (2013). [Abstract]
  • Verghese, P.B., Castellano, J.M., Garai, K., Wang, Y., Jiang, H., Shah, A., Bu, G., Frieden, C. and Holtzmann, D.M. ApoE influences amyloid-β (Aβ) clearance despite minimal apoE/Aβ association in physiological conditions. PNAS 110:E1807-1816 (2013). [Abstract]
  • Garai, K. and Frieden, C. Quantitative analysis of the time course of Aβ oligomerization and subsequent growth steps using tetramethylrhodamine-labeled Aβ. PNAS 110:3321-3326 (2013). [Abstract]
  • Frieden, C. and Garai, K. Structural differences between apoE3 and apoE4 may be useful in developing therapeutic agents for Alzheimer’s disease. PNAS 109:8913-8918 (2012). [Abstract]
  • Shu, Q., Crick, S.L., Pinkner, J.S., Ford, B., Hultgren, S.J. and Frieden, C. The E. coli CsgB nucleator of curli assembles to beta-sheet oligomers that alter the CsgA fibrillization mechanism. PNAS 109:6502-6507 (2012). [Abstract]
  • Huang, R.Y., Garai, K., Frieden, C. and Gross, M.L. Hydrogen/deuterium exchange and electron-transfer dissociation mass spectrometry determine the interface and dynamics of apolipoprotein E oligomerization. Biochemistry 50:9273-9282 (2011). [Abstract]
  • Gau, B.C., Garai, K., Frieden, C. and Gross, M.L. Mass spectrometry-based protein footprinting characterizes the structures of oligomeric apolipoprotein E2, E3, and E4. Biochemistry 50:8117-8126 (2011). [Abstract]
  • Garai, K., Baban, B. and Frieden, C. The self-association and stability of the APOE isoforms at low pH: Implications for APOE-lipid interactions. Biochemistry 50:6356-6364 (2011). [Abstract]
  • Garai, K., Baban, B. and Frieden, C. Dissociation of apolipoprotein E oligomers to monomer is required for high-affinity binding to phospholipid vesicles. Biochemistry 50:2550-2558 (2011). [Abstract]
  • Garai, K. and Frieden, C. The association-dissociation behavior of the ApoE proteins: Kinetic and equilibrium studies. Biochemistry 49:9533-9541 (2010). [Abstract]
  • Frieden, C. Sidney Frederick Velick. Biogr Mem Natl Acad Sci. (2010).
  • Niu, W., Shu, Q., Chen, Z., Mathews, S., Di Cera, E. and Frieden, C. The role of Zn(2+) on the structure and stability of murine adenosine deaminase. J Phys Chem B 114:16156-16165 (2010). [Abstract]
  • Baldwin, R.L., Frieden, C. and Rose, G.D. Dry molten globule intermediates and the mechanism of protein unfolding. Proteins 78:2725-2737 (2010). [Abstract]
  • Mustafi, S.M., Garai, K., Crick, S.L., Baban, B. and Frieden, C. Substoichiometric inhibition of Abeta(1-40) aggregation by a tandem Abeta(40-1-Gly8-1-40) peptide. Biochem Biophys Res Commun 397:509-512 (2010). [Abstract]
  • Garai, K., Mustafi, S.M., Baban, B. and Frieden, C. Structural differences between apolipoprotein E3 and E4 as measured by (19)F NMR. Protein Sci. 19:66-74. (2010). [Abstract]

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