Backbone resonance assignment of PDI b'xa' domain construct

Human protein disulfide isomerase (PDI), a protein containing 4 domains a, b, b′, a′, disordered x linker and C-terminus, plays critical roles in disulfide bond reactions and proper protein folding in the endoplasmic reticulum. The bb′ domain contributes to client binding, the a, a′ domain catalyse the rearrangement of the disulfide bonds. The x linker and a′ domain were the main dynamics region for full-length PDI and the b′xa′ construct has the minimum functional domain within full-length PDI. Herein, we report a new preparation strategy with 1, 6-hexandiol and backbone NMR chemical shift assignments for the monomer b′xa′ domain.