Interhelical

Interhelical refers to the space or interaction between alpha-helices, which are common secondary structures found in proteins. Alpha-helices are coiled, rod-like structures formed by a polypeptide chain. When two or more of these helices are positioned near each other within a protein's three-dimensional structure, the regions between them are considered interhelical. These interhelical spaces can be important for protein function. They may contain binding sites for other molecules, such as ligands or other proteins, or they can be involved in the formation of protein complexes. The nature of the amino acid residues lining the interhelical regions dictates their chemical properties and thus their potential interactions. Hydrophobic residues facing inwards might create a nonpolar core, while charged or polar residues on the exterior could interact with the surrounding aqueous environment or other charged molecules. The precise arrangement and distance between helices in these interhelical regions are crucial for maintaining the overall stability and functionality of the protein. Understanding interhelical interactions is therefore a key aspect of protein folding and molecular recognition.