rotameric

Rotameric refers to the different low-energy conformations that a molecule can adopt due to the rotation around single bonds. This concept is particularly relevant in the study of proteins and other biomolecules, where the spatial arrangement of atoms and functional groups can significantly influence the molecule's properties and interactions. The term "rotamer" was coined by Linus Pauling in 1960 to describe these alternative conformations.

The rotameric states of a molecule are determined by the torsional angles around single bonds, which can vary due to the free rotation around these bonds. However, not all rotational angles are equally probable; certain angles correspond to lower energy states, known as rotamers. These rotamers can have a profound impact on the molecule's biological activity, stability, and interactions with other molecules.

In proteins, for example, the rotameric states of amino acid side chains can influence protein folding, enzyme activity, and molecular recognition. The study of rotameric states is crucial in fields such as structural biology, medicinal chemistry, and drug design, as it helps in understanding the structural basis of molecular interactions and in designing molecules with desired properties.