Structural, ligand binding and redox studies of hPDI fragments using NMR spectroscopy
Human Protein Disulphide Isomerase (hPDI) is an important protein folding catalyst involved in the reduction, oxidation and isomerisation of disulphide bonds, a major rate-limiting step in the formation of many proteins. hPDI also exhibits molecular chaperone activity, selectively binding small, unf...
| Main Author: | |
|---|---|
| Other Authors: | |
| Published: |
University of Kent
2015
|
| Subjects: | |
| Online Access: | https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.695688 |