allosteric protein

allosteric protein

A protein that changes from one folding conformation to a different shape when another molecule binds to it. The change in conformation alters the activity or properties of the protein.
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Ostermeier, "Engineering allosteric protein switches by domain insertion," Protein Engineering, Design and Selection, vol.
Therefore, Hbs were considered as a sort of 'obliged' allosteric protein complexes and, even thanks to the great amount of both structural and physiological data, attracted a lot of attentions [8-10].
Allosteric changes can be induced by binding the protein to another protein called a ligand, while the allosteric protein that changes shape is often a receptor.
Hb is an allosteric protein that undergoes conformational change in quaternary structure from the T (tense) state (deoxy-Hb) to the R (relaxed) state (oxy-Hb) upon binding its first oxygen molecule such that the binding of additional oxygen molecules is enhanced.
Changeux and Edelstein, who were significant contributors to research on the nicotinic receptors for acetylcholine (a membrane associated with chemical transduction in the nervous system that also interfaces with nicotine) and allosteric proteins. They review the most recent experiments and theoretical breakthroughs, while describing their interest and excitement about this groundbreaking work.