dept of biochemistry and molecular biophysics




Faculty

picture of Carl Frieden
Carl Frieden
 Professor of Biochemistry and Molecular Biophysics
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

  • 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).

  • Crick, S.L, Jayaraman, M., Frieden, C., Wetzel, R. and Pappu, R.V. Fluorescence correlation spectroscopy shows that monomeric polyglutamine molecules form collapsed structures in aqueous solutions. Proc Natl Acad Sci USA 103:16764-16769 (2006).

  • Li, H . and Frieden, C. Fluorine-19 NMR studies on the acid state of the intestinal fatty acid binding protein. Biochemistry 45:6272-6278 (2006).

  • Chattopadhyay, K. and Frieden, C. Steady-state and time-resolved fluorescence studies of the intestinal fatty acid binding protein. Proteins 63:327-335 (2006).

  • Justice, S. S., Hunstad, D. A., Harper, J. R., Duguay, A. R., Pinkner, J. S., Bann, J., Frieden, C., Silhavy, T. J. and Hultgren, S. J. Periplasmic peptidyl prolyl cis-trans isomerases are not essential for viability, but SurA is required for pilus biogenesis in Escherichia coli. J Bacteriol 187:7680-7686 (2005).

 

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