Final answer:
The statement that many protein molecules are allosteric is true. Allosteric regulation applies to various proteins, including receptors, transport proteins, and structural proteins, and it involves the binding of modulators at allosteric sites leading to functional changes.
Step-by-step explanation:
The statement that many protein molecules (not just enzymes) are allosteric is true. Allosteric regulation is not unique to enzymes; it can also apply to other proteins that undergo conformational changes upon ligand binding at sites other than the active or binding site, leading to a change in their activity or function.
Allosteric regulation is a key aspect in the control of various biochemical pathways, allowing for fine-tuning of cellular processes. Proteins that are allosterically regulated may have allosteric sites where small molecules, ions, or other proteins bind, leading to a change in the protein's structure and its activity.
All types of proteins, including receptors, transport proteins, and even structural proteins, can potentially exhibit allosteric properties if their function can be modulated in this way.
For example, some receptor proteins on cell membranes can have allosteric sites where modulators bind, leading to changes in the receptor's shape and influencing its ability to bind to its primary ligand.