Supplementary MaterialsSupplementary_Info 41598_2017_3966_MOESM1_ESM. evaluation of DRIN in oxidized and decreased states

Supplementary MaterialsSupplementary_Info 41598_2017_3966_MOESM1_ESM. evaluation of DRIN in oxidized and decreased states reveals stores of residue connections that signify potential allosteric pathways between catalytic and ligand binding sites of hPDI. Launch The human proteins disulfide isomerase (hPDI), is among the most abundant redox-regulated molecular chaperones accounting for the folding of nearly one-third of proteins in cells1.… Continue reading Supplementary MaterialsSupplementary_Info 41598_2017_3966_MOESM1_ESM. evaluation of DRIN in oxidized and decreased states