[28] Thermodynamic approaches to understanding aspartate transcarbamylase
- 1 January 1995
- book chapter
- Published by Elsevier
- Vol. 259, 608-628
- https://doi.org/10.1016/0076-6879(95)59064-1
Abstract
No abstract availableThis publication has 59 references indexed in Scilit:
- Molecular Code for Cooperativity in HemoglobinScience, 1992
- Escherichia coli Aspartate Transcarbamoylase: Structure, Energetics, and Catalytic and Regulatory MechanismsAnnual Review of Biophysics, 1989
- Analysis of the ligand-promoted global conformational change in aspartate transcarbamoylaseJournal of Molecular Biology, 1989
- Free energy coupling within macromoleculesJournal of Molecular Biology, 1983
- Interactions of ionizable groups in E. coli aspartate transcarbamylase with adenosine and cytidine 5'-triphosphatesBiochemistry, 1982
- On the detection of homotropic effects in enzymes of low co-operativity. Application to modified aspartate transcarbamoylaseJournal of Molecular Biology, 1981
- Calorimetric analysis of aspartate transcarbamylase from Escherichia coli. Binding of substrates and substrate analogs to the native enzyme and catalytic subunitBiochemistry, 1978
- Subunit interactions in aspartate transcarbamylase from Escherichia coli studied using matrix‐bound derivativesFEBS Letters, 1974
- Binding of cytidine triphosphate to aspartate transcarbamylaseBiochemical and Biophysical Research Communications, 1970
- On the nature of allosteric transitions: A plausible modelJournal of Molecular Biology, 1965