Molecular chaperones are abundant and conserved proteins in the cytosol, mitochondria, nucleus and endoplasmic reticulum that help protein clients fold to their active conformation known as the native state. The structure and mechanism of these chaperones holds significance because of their association with cancer and metabolic disease. The heat shock protein 70 (Hsp70) family of […]
A42: Implications of ERdj6 Mutation on Co-Chaperone Ability and Oligomerization
Within the field of biochemistry, chaperone and co-chaperone proteins are of important significance due to their vital role in assisting protein folding. ERdj6 is an Hsp40 co-chaperone that works with Hsp70 to facilitate client binding and folding. ERdj6 was grown and purified in E. Coli, with wild-type and mutant protein samples grown. Within Hsp40 proteins […]