Joseph R. Mattingly
Teaching Specialist, MBB
Ph.D. University of Notre Dame
Office: 421 SCB
Phone: (816) 235-2258
E-mail: MattinglyJ
Research Areas
Protein engineering by rational design and directed in vitro evolution, biophysical studies of protein folding, proteomics, protein-protein interactions.
Current Interests
"Perhaps the last great remaining question in molecular biology is how the linear amino acid sequence of a protein directs it to fold into the three dimensional structure it needs for biological activity. Pioneering studies revealed that purified proteins can fold autonomously in the test tube. More recent studies have revealed that other proteins, generically known as chaperones, can often assist the refolding of many newly synthesized proteins in the cell. We are studying the factors that determine when, where, and how various chaperones assist protein folding in this complex environment. "
"Our studies focus primarily on proteins that are synthesized in the cell cytoplasm and then transported into the mitochondrion. The folding of such proteins must be carefully regulated, since premature folding will prevent their translocation across the outer and inner mitochondrial membranes. We study this regulation by using rational design mutagenesis and directed in vitro evolution to alter the amino acid sequence of proteins and change their rates of folding while not interfering with their biological activity. We are also investigating affinity-tagging methods for identifying which chaperones bind to these engineered nascent proteins."
"Though these studies have relevance to the protein folding problem in general, they also address a biomedical problem-namely, how to cure mitochondriopathies by delivery of proteins into the mitochondrion. "
