A Native‐Like Intermediate on the Ribonuclease A Folding Pathway
- 1 February 1981
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 114 (1), 105-109
- https://doi.org/10.1111/j.1432-1033.1981.tb06179.x
Abstract
No abstract availableThis publication has 19 references indexed in Scilit:
- Role of proline isomerization in folding of ribonuclease A at low temperaturesProceedings of the National Academy of Sciences, 1979
- Detection of an early intermediate in the folding of ribonuclease A by protection of amide protons against exchangeJournal of Molecular Biology, 1979
- Acid catalysis of the formation of the slow-folding species of RNase A: Evidence that the reaction is proline isomerizationProceedings of the National Academy of Sciences, 1978
- Test of the extended two-state model for the kinetic intermediates observed in the folding transition of ribonuclease AJournal of Molecular Biology, 1978
- Nuclear magnetic resonance evidence for a structural intermediate at an early stage in the refolding of ribonuclease AJournal of Molecular Biology, 1978
- Guanidine-unfolded state of ribonuclease A contains both fast- and slow-refolding species.Proceedings of the National Academy of Sciences, 1976
- Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residuesBiochemistry, 1975
- Both the Fast and Slow Refolding Reactions of Ribonuclease A Yield Native EnzymeProceedings of the National Academy of Sciences, 1973
- Spectrophotometric assay of bovine pancreatic ribonuclease by the use of cytidine 2′:3′-phosphateBiochemical Journal, 1960
- Some spectrophotometric and polarimetric experiments with ribonucleaseBiochimica et Biophysica Acta, 1957