Detection of intermediates in protein folding of carbonic anhydrase with fluorescence emission and polarization.
Open Access
- 1 November 1978
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 253 (22) , 8016-8018
- https://doi.org/10.1016/s0021-9258(17)34354-5
Abstract
No abstract availableThis publication has 9 references indexed in Scilit:
- The pathway of protein foldingTrends in Biochemical Sciences, 1978
- Nuclear magnetic resonance evidence for a structural intermediate at an early stage in the refolding of ribonuclease AJournal of Molecular Biology, 1978
- Unfolding and refolding occur much faster for a proline-free proteins than for most proline-containing proteins.Proceedings of the National Academy of Sciences, 1977
- Cis‐Trans equilibrium and kinetic studies of acetyl‐L‐proline and glycyl‐L‐prolineBiopolymers, 1977
- Kinetics and mechanism of refolding of bovine carbonic anhydrase. A probe study of the formation of the active siteBiochemistry, 1977
- Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residuesBiochemistry, 1975
- Kinetics of refolding of guanidine hydrochloride denatured cytochrome c. Temperature dependenceBiochemistry, 1973
- Role of zinc(II) in the refolding of guanidine hydrochloride denatured bovine carbonic anhydraseBiochemistry, 1972
- Crystal Structure of Human Carbonic Anhydrase CNature New Biology, 1972