Mechanisms of protein folding

From the Frieden lab: The mechanism of protein folding, the role of chaperones in the folding process, the relation of protein structure to function and measurements of protein dynamics are projects under study in this laboratory. The long-term goal of the protein folding work is to understand the nature of the intermediate structures on the unfolding and refolding pathways. Work in the laboratory uses site-directed mutagenesis and techniques such as 19F and proton NMR, circular dichroism, fluorescence measurements and other biophysical methods. Shown here is one of the proteins under study called PapD. This protein is required for the formation of pili in pathogenic bacteria but functions as a chaperone for the folding of other protein subunits that make up the pilus structure. The protein has two distinct domains and real-time NMR experiments show that that there must be domain-domain interaction for correct folding of the protein.

Click to view full-size image…