Ostermeier, "Engineering
allosteric protein switches by domain insertion," Protein Engineering, Design and Selection, vol.
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.