Protein Folding: Folding helpers and unhelpful folders
- 31 October 1994
- journal article
- Published by Elsevier in Current Biology
- Vol. 4 (10) , 933-935
- https://doi.org/10.1016/s0960-9822(00)00210-4
Abstract
No abstract availableKeywords
This publication has 7 references indexed in Scilit:
- Dissecting the Mechanism of Protein Disulfide Isomerase: Catalysis of Disulfide Bond Formation in a Model PeptideBiochemistry, 1994
- Intact Disulfide Bonds Decelerate the Folding of Ribonuclease T1Journal of Molecular Biology, 1994
- Native disulfide bonds greatly accelerate secondary structure formation in the folding of lysozymeProtein Science, 1994
- Reactivity and Ionization of the Active Site Cysteine Residues of DsbA, a Protein Required for Disulfide Bond Formation in vivoBiochemistry, 1994
- Effects of DsbA on the Disulfide Folding of Bovine Pancreatic Trypsin Inhibitor and .alpha.-LactalbuminBiochemistry, 1994
- Replacement of the Active-Site Cysteine Residues of DsbA, a Protein Required for Disulfide Bond Formation in vivoBiochemistry, 1994
- A model catalyst of protein disulphide bond formationCurrent Biology, 1993