Two slow stages in refolding of bovine carbonic anhydrase B are due to proline isomerization
- 1 June 1990
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 213 (3), 561-568
- https://doi.org/10.1016/s0022-2836(05)80215-3
Abstract
No abstract availableThis publication has 26 references indexed in Scilit:
- Catalysis of protein folding by prolyl isomeraseNature, 1987
- The refolding of urea-denatured ribonuclease A is catalyzed by peptidyl-prolyl cis-trans isomeraseBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1985
- Conformational specificity of chymotrypsin toward proline-containing substratesBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1984
- ‘Molten‐globule“ state accumulates in carbonic anhydrase foldingFEBS Letters, 1984
- The conformation around the peptide bond between the P1- and P2-positions is important for catalytic activity of some proline-specific proteasesBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1983
- Specific Intermediates in the Folding Reactions of Small Proteins and the Mechanism of Protein FoldingAnnual Review of Biochemistry, 1982
- Possible implications of many proline residues for the kinetics of protein unfolding and refoldingJournal of Molecular Biology, 1978
- The pathway of protein foldingTrends in Biochemical Sciences, 1978
- Cis‐Trans equilibrium and kinetic studies of acetyl‐L‐proline and glycyl‐L‐prolineBiopolymers, 1977
- Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residuesBiochemistry, 1975