The thermodynamics of binding involves understanding the energetic changes that occur when two molecules, such as a ligand and a protein, interact to form a stable complex. This process is governed by principles of enthalpy, entropy, and free energy, which together determine the affinity and specificity of the binding interaction.
Conformational change refers to the alteration of the shape of a macromolecule, often a protein or nucleic acid, in response to environmental factors or binding events, which can significantly impact its function and interactions. These structural transitions are crucial in biological processes such as enzyme catalysis, signal transduction, and molecular recognition, allowing dynamic regulation of cellular activities.