How is the confirmation of a protein directly linked to its function?

One or more polypeptides that have been coiled and folded into a specific shape make up a functional protein; even a small alteration in a protein's primary structure can have an impact on the protein's conformation and, consequently, its functionality.

For instance: 1) enzymes recognize and bind to specific substrates, facilitating a chemical reaction; 2) antibodies bind to specific foreign substances that fit their binding sites; and 3) neurotransmitters transmit signals from one cell to another by binding to receptor sites on proteins in the receiving cell's membrane.

Understanding the conformation of proteins is crucial to understanding the interactions between biomolecules. A loss of 3-D structure can cause a protein to malfunction or cause dangerous diseases. For instance, in sickle cell anemia patients, a single amino acid substitution can lead to the development of abnormal hemoglobin.

A protein's three-dimensional structure dictates how it specifically interacts with other molecules, including substrates and other proteins, and this structure is essential for the protein to perform its biological functions, such as enzyme activity, receptor binding, and structural support. Modest changes in protein conformation can have a substantial impact on the function of the protein, potentially affecting biological processes and overall cellular function. Therefore, the confirmation of a protein has a direct impact on its function.