Comparison of active mutants and wild-type aspartate transcarbamoylase of Escherichia coli.
Open Access
- 31 August 1984
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 259 (17) , 11027-11035
- https://doi.org/10.1016/s0021-9258(18)90617-4
Abstract
No abstract availableThis publication has 62 references indexed in Scilit:
- Calorimetric study of tryptophan synthase α‐subunit and two mutant proteinsInternational Journal of Peptide and Protein Research, 1982
- Effect of single amino acid substitutions at the same position on stability of a two-domain proteinJournal of Molecular Biology, 1982
- Analysis of mutant Escherichia coli aspartate transcarbamylases isolated from a series of suppressed pyrB nonsense strainsJournal of Molecular Biology, 1981
- On the detection of homotropic effects in enzymes of low co-operativity. Application to modified aspartate transcarbamoylaseJournal of Molecular Biology, 1981
- pH dependence of stability of the wild-type tryptophan synthase α-subunit and two mutant proteins (Glu49 → Met or Gln)Journal of Molecular Biology, 1980
- Changes in the X-ray solution scattering of aspartate transcarbamylase following the allosteric transitionJournal of Molecular Biology, 1979
- Genetic studies of the lac repressorJournal of Molecular Biology, 1977
- A thermodynamic approach to the problem of stabilization of globular protein structure: A calorimetric studyJournal of Molecular Biology, 1974
- On the nature of allosteric transitions: A plausible modelJournal of Molecular Biology, 1965
- Coordination of the synthesis of the enzymes in the pyrimidine pathway of E. coliJournal of Molecular Biology, 1962