Understanding the role of proline isomerization in ribonuclease T1 folding

From the Frieden lab: Protein folding and aggregation are under study in this laboratory. The long-term goal of the 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. Current studies include the incorporation of fluoroproline into proteins to examine the role of proline isomerization in folding as followed by NMR. Shown here is one such protein under study, ribonuclease T1. The laboratory is also studying, by the same techniques, the properties of those proteins and peptides characterized as intrinsically disordered. These peptides/proteins are involved with the formation of aggregates found in diseases such as Alzheimer’s, Parkinson’s and Huntington’s.

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