Allostery
Description
Allostery is a form of regulation, in which enzymatic activity is modulated through the binding of an effector molecule. Effector binding mediates a conformational change that stabilizes either the low activity T state or high activity R state, thereby impacting catalytic function. Aspartate transcarbamoylase (ATCase) is one example of a well studied allosteric protein.
Acknowledgements
References
Hodges, M., Barahona, M. & Yaliraki, S.N. Allostery and cooperativity in multimeric proteins: bond-to-bond propensities in ATCase. Sci Rep 8, 11079 (2018). https://doi.org/10.1038/s41598-018-27992-z
Nelson, D. L., & Cox, M. M. (2017). Lehninger principles of biochemistry (7th ed.). W.H. Freeman.
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