Carl Frieden, Ph.D.

DEPARTMENT OF Biochemistry & Molecular Biophysics
Keywords: biophysics, kinetics, protein folding, NMR, fluorescence, intrinsically disordered proteins

The mechanism of protein folding is poorly understood. What is the nature of folding intermediates and what are the determinants that control correct folding rather than misfolding. How do dynamics in the unfolded state control the folding process. What is the nature of intrinsically disordered proteins that form aggregates leading to neurodegerative diseases. These are the questions being addressed in this laboratory.

The long-term goal of the protein folding work is to understand the nature of the intermediate structures on the unfolding, refolding and aggregation pathways. Work in the laboratory uses site-directed mutagenesis and techniques such as ¹⁹F and proton NMR, circular dichroism, state-of–the-art fluorescence measurements and other biophysical methods. Of particular interest are methods that allow determination of the time dependence of motions in native and unfolded proteins. A variety of proteins are used to address these questions.