Alteration Around the Active Site of Rhodanese during Urea-induced Denaturation and Its Implications for Folding
Open Access
- 1 May 2000
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 275 (20) , 14860-14864
- https://doi.org/10.1074/jbc.275.20.14860
Abstract
No abstract availableKeywords
This publication has 25 references indexed in Scilit:
- Domain Separation Precedes Global Unfolding of RhodanesePublished by Elsevier ,1999
- Protein folding in the cellNature, 1992
- Unfolding-refolding transition of a hinge bending enzyme: horse muscle phosphoglycerate kinase induced by guanidine hydrochlorideBiochemistry, 1984
- Evidence for intermediates during unfolding and refolding of a two-domain protein: phage T4 lysozyme equilibrium and kinetic studiesBiochemistry, 1984
- The high resolution three-dimensional structure of bovine liver rhodaneseFundamental and Applied Toxicology, 1983
- The covalent and tertiary structure of bovine liver rhodaneseNature, 1978
- Subcellular distribution and intramitochondrial localization of three sulfurtransferases in rat liverFEBS Letters, 1975
- ErrataBiochemical and Biophysical Research Communications, 1974
- Enhancement of rhodanese activity during controlled digestion with trypsinBiochemical and Biophysical Research Communications, 1974
- Low-molecular Carbohydrates in Algae. II. Synthesis of 1-D-Mannitol Monoacetate and 1,6-D-Mannitol Diacetate.Acta Chemica Scandinavica, 1953