Role of an evolutionarily invariant serine for the stability of human carbonic anhydrase II
- 1 January 1992
- journal article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
- Vol. 1118 (2) , 179-186
- https://doi.org/10.1016/0167-4838(92)90148-7
Abstract
No abstract availableKeywords
This publication has 21 references indexed in Scilit:
- Strategy for analysing the co-operativity of intramolecular interactions in peptides and proteinsJournal of Molecular Biology, 1990
- Conformational Properties of the Amino Acid Residues L-Cysteine, L-Serine and L-Cystine.Acta Chemica Scandinavica, 1990
- The role of the metal ion in the refolding of denatured bovine Co(II)-carbonic anhydrase IIBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1989
- Production of Active Human Carbonic Anhydrase II in E. Coli.Acta Chemica Scandinavica, 1988
- Origins and Molecular Evolution of the Carbonic Anhydrase IsozymesaAnnals of the New York Academy of Sciences, 1984
- Kinetics and Mechanism of Carbonic Anhydrase IsoenzymesaAnnals of the New York Academy of Sciences, 1984
- Conformational stability of mixed disulfide derivatives of .beta.-lactoglobulin BBiochemistry, 1983
- Carbon-13 nuclear magnetic resonance probe of active-site ionizations in human carbonic anhydrase BBiochemistry, 1977
- Probes for the Conformational Transitions of Phosphorylase bEuropean Journal of Biochemistry, 1971
- The reactivity of SH groups with a fluorogenic reagentFEBS Letters, 1970