Conformation

A molecular shape produced by rotation around single bonds without breaking covalent bonds. Different conformations can vary in energy and affect a molecule’s properties and reactivity.

Torsion angle: The angle between two planes defined by four consecutively bonded atoms. It measures rotation around a bond and distinguishes conformations.
Single bond: A covalent bond formed by one shared electron pair, typically permitting rotation around its bond axis. Rotation around single bonds generates the shapes called conformations.
Protein folding: The process by which a protein chain adopts a three-dimensional structure. Folding selects a functional arrangement from many possible conformations.
Configuration (chemistry): The fixed spatial arrangement of atoms in a molecule that cannot change without breaking or reforming bonds. Unlike conformations, configurations cannot interconvert through ordinary single-bond rotation.
Conformational analysis: The study of molecular shapes, their relative energies, and interconversion. It compares the conformations accessible through bond rotation.
Steric hindrance: An increase in energy or reduced reactivity caused by atoms crowding one another in space. Crowded arrangements disfavor some conformations.
Induced fit: A model in which ligand binding prompts a protein to change shape and improve the interaction. Binding can shift a protein into a different conformation.
Constitutional isomer: One of two or more compounds with the same molecular formula but different atom-to-atom connectivity. Conformations preserve connectivity; constitutional isomers do not share it.
Potential energy surface: A function assigning potential energy to each configuration of a molecular system. Its energy minima and barriers describe favored conformations and their interconversion.
Van der Waals interaction: A set of weak attractive and repulsive forces between atoms or molecules. These interactions contribute to the relative energies of molecular shapes.

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