Department of Biochemistry and Molecular Biophysics at Washington University School of Medicine in St. Louis, MO Washington University School of Medicine in St. Louis, MO Washington University in St. Louis, MO




Faculty


carl frieden

Carl Frieden


Professor
Dept. of Biochemistry and
Molecular Biophysics

Office: 215 McDonnell Science Building
Phone: 314-362-3344
Fax: 314-362-7183
Email: frieden@biochem.wustl.edu

Lab Website
Research Opportunities

Mailing Address:
WUSM - Biochemistry Dept.
660 S. Euclid Ave., MS8231
St. Louis, MO 63110



Research Interests

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



Selected Publications

  • Hu, X., Crick, S.L., Bu, G., Frieden, C., Pappu, R.V. and Lee, J.M. Amyloid seeds formed by cellular uptake, concentration, and aggregation of the amyloid-beta peptide. Proc Natl Acad Sci USA (E-pub ahead of print.) (2009).

  • Garai, K., Mustafi, S.M., Baban, B. and Frieden, C. Structural differences between apoli proprotein E3 and E4 as measured by (19)F- NMR. Protein Sci (E-pub ahead of print.) (2009).

  • Zhang, R., Hu, X., Khant, H., Ludtke, S.J., Chiu, W., Schmeid, M.F., Frieden, C. and Lee, J.M. Interprotofiliment interactions between Alzheimer's A{beta}1-42 peptides in amyloid fibrils revealed by cryoEM. PNAS 106:4653-4658 (2009).

  • Garai, K., Crick, S.L., Mustafi, S.M. and Frieden, C. Expression and purification of amyloid-beta peptides from Escherichia coli. Protein Expr Purif. 66:107-112 (2009).

  • Frieden, C. A lifetime of kinetics. J Biol Chem. 283:19873-19878 (2008).

  • Frieden, C. Protein aggregation Processes: In search of the mechanism. Protein Science16:2334-2344 (2007).

  • Li, H. and Frieden, C. Observation of sequential steps in the folding of intestinal fatty acid binding protein using a slow folding mutant and 19F NMR. Proc Natl Acad Sci USA 104:11993-11998 (2007).

  • Li, H. and Frieden, C. Comparison of C40/82A and P27A C40/82A Barstar mutants using (19)F NMR. Biochemistry 46:4337-4347 (2007).

 

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