Carl Frieden, Ph.D.

Washington University
School of Medicine

Dept. of Biochemistry & Molecular Biophysics
Box 8231
660 S. Euclid Ave.
St. Louis, MO 63110

tel: (314) 362-3344
fax: (314) 362-7183
email: frieden@wustl.edu
web: Personal Weblink

 

 

RESEARCH INTEREST

A major focus of our work has been to understand the role of structural elements (i.e., turns, strands and helices) of the rat intestinal fatty acid binding protein in the folding process using NMR techniques. The mutant proteins generated for analysis of folding pathways have also being used to analyze ligand protein interactions and membrane-protein interactions to understand the biophysical mechanisms involved in intercellular trafficking of fatty acids. Recently we have developed novel approach using fluorescence correlation spectroscopy in association with fluorescence resonance energy transfer to measure microsecond dynamic motion in native intestinal fatty acid binding protein as well as unfolded forms.

SELECTED PUBLICATIONS

Rajabzadeh M, Kao J, Frieden C. Consequences of single-site mutations in the intestinal fatty acid binding protein. Biochemistry. 2003;42:12192-9.

Chattopadhyay K, Saffarian S, Elson EL, Frieden C. Measurement of microsecond dynamic motion in the intestinal fatty acid binding protein by using fluorescence correlation spectroscopy. Proc Natl Acad Sci U S A. 2002;99:14171-6.

Nikiforovich GV, Frieden C. The search for local native-like nucleation centers in the unfolded state of beta -sheet proteins. Proc Natl Acad Sci U S A. 2002; 99:10388-93.

Chattopadhyay K, Zhong S, Yeh SR, Rousseau DL, Frieden C. The intestinal fatty acid binding protein: the role of turns in fast and slow folding processes. Biochemistry. 2002; 41:4040-7.