Thermodynamics of Protein Folding

The thermodynamics of protein folding involves understanding how proteins change from an unstructured chain to a specific, functional shape. This process depends on a balance of energy and disorder: folding releases energy (making it favorable) but also decreases entropy (disorder), which opposes folding. Proteins fold spontaneously because the overall energy change—considering both factors—is negative, resulting in a stable, minimal-energy structure. This balance ensures proteins assume their correct shapes, crucial for their biological functions. Basically, protein folding is a natural quest for the most energetically favorable, ordered state amid competing forces.