Computational Modeling of Chaperone Interactions in the Endoplasmic Reticulum of Saccharomyces Cerevisiae

In eukaryotes, the endoplasmic reticulum (ER) acts as a protein gatekeeper for protein folding, maturation, and transport. Molecular chaperones, of the Hsp70 family of proteins, participate in assisting these processes and are essential to cellular function and survival. BiP is the resident chaperone in the ER of Sacchromyces cerevisiae. In this study we have created two deterministic models to examine how BiP interacts with the membrane-bound co-chaperone Sec63 in translocation, a process in which BiP assists in guiding a nascent protein into the ER lumen.