Protein Processing and Folding

All newly-synthesized polypeptides have to be folded into their three-dimensional structures to be functional. Many proteins have to reach destinations other than the cytosol, the site where protein synthesis occurs. In addition, a majority of proteins undergo post-translational modification in response to a wide variety of cellular signals. Therefore, understanding the mechanism and regulation of protein folding, protein translocation, and protein processing is an integral part of modern molecular and cell biology. In addition, errors in these processes cause diseases ranging from Alzheimer's to diabetes. Protein folding and processing is one of the major research focuses in our department. Faculty in this area engage in a number of research topics including the unfolded protein response, the human blood clotting system, the structure and function of molecular chaperones, the heat shock response, protein misfolding in aging and disease, yeast pheromone processing, protein transport in the secretory pathway, protein targeting, organelle biogenesis, and protein design and engineering.

Primary Faculty

Philip Andrews, Ph.D.

Protein interactions and the role of post-translational modifications in controlling these interactions

Ryan Baldridge, Ph.D.

Mechanisms of membrane-bound protein quality control systems

Robert Fuller, Ph.D.

Protein localization and processing in the eukaryotic secretory pathway

Phyllis Hanson, M.D., Ph.D.

Protein-protein and protein-membrane interactions involved in membrane trafficking and organelle structure

James Morrissey, Ph.D.

Biochemistry of the human blood clotting system; structural studies of protein-membrane complexes

Stephen Ragsdale, Ph.D.

Interactions and processing of proteins involved in heme metabolism, the circadian clock, the global carbon cycle, and methylmercury

Zhaohui Xu, Ph.D.

Structural biology and molecular mechanisms of protein folding and trafficking in eukaryotic cells

Secondary Joint Faculty

James Bardwell, Ph.D.

Roles of molecular chaperones and disulfide catalysts in protein folding; experimental evolution of protein folding

Ursula Jakob, Ph.D.

Biochemical aspects of the bacterial response to oxidative stress

Yang Zhang, Ph.D.

Development of advanced bioinformatics methods to predict 3-dimensional structures of proteins from amino acid sequences and deduce the biological functions based on the sequence-to-structure-to-function paradigm; protein design (or inverse protein folding); protein-ligand docking; drug discovery