One of the most important components of proteins is the alpha helix, a structure composed of repeating alpha turns commonly believed to be the same. However alpha turns are not all the same, different types existing at ends or kinks of helices, as reverse turns in beta sheets, or alone as isolated structural motifs. Alpha turns are often exposed at sites recognized by other proteins. This study will analyse protein structures for different alpha turn types, create the first small molecules designed to stabilise each alpha turn type, and characterise their chemical, structural and biological properties. Results will fill a gap in our knowledge of protein/peptide structure, and inform new designs of pharmaceuticals, vaccines and materials.