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Protein disulfide isomerase (PDI) is a protein-folding assistant and a molecular chaperone found in the endoplasmic reticulum. This enzyme catalyzes the formation and the isomerization of disulfide bonds. The binding and release of substrate from molecular chaperones are usually triggered by cycles of ATP hydrolysis. It has been proposed that the substrate binding / release cycle of PDI could be correlated with the redox states of its active sites. This book examines the differences between the domains that compose PDI in regards to their functions and the consequences of the conformational alteration they experience upon redox condition changes. (Imprint: Nova)