Noncooperative temperature melting of a globular protein without specific tertiary structure: Acid form of bovine carbonic anhydrase B
- 1 October 1985
- journal article
- research article
- Published by Wiley in Biopolymers
- Vol. 24 (10), 1899-1907
- https://doi.org/10.1002/bip.360241005
Abstract
No abstract availableThis publication has 18 references indexed in Scilit:
- ‘Molten‐globule“ state accumulates in carbonic anhydrase foldingFEBS Letters, 1984
- ‘Molten‐globule state’: a compact form of globular proteins with mobile side‐chainsFEBS Letters, 1983
- Detection and characterization using circular dichroism and fluorescence spectroscopy of a stable intermediate conformation formed in the denaturation of bovine carbonic anhydrase with guanidinium chlorideBiochemistry, 1982
- α‐lactalbumin: compact state with fluctuating tertiary structure?FEBS Letters, 1981
- Multiparameter kinetic study on the unfolding and refolding of bovine carbonic anhydrase BBiochemistry, 1980
- The use of deuterium exchange for the study of the distortion of α-helices in proteinsJournal of Molecular Biology, 1978
- Intramolecular distortion of the α-helical structure of polypeptidesJournal of Molecular Biology, 1976
- Intensities and other spectral parameters of infrared amide bands of polypeptides in the α‐helical formBiopolymers, 1974
- Acid denaturation of bovine carbonic anhydrase BBiochemistry, 1974
- Intensities and other spectral parameters of infrared amide bands of polypeptides in the β‐ and random formsBiopolymers, 1973