Transmembrane β‐peptide helices as molecular rulers at the membrane surface

β‐Peptides are known to form 14‐helices with high conformational rigidity, helical persistence length, and well‐defined spacing and orientation regularity of amino acid side chains. Therefore, β‐peptides are well suited to serve as backbone structures for molecular rulers. On the one hand, they can be functionalized in a site‐specific manner with molecular probes or fluorophores, and on the other hand, the β‐peptide helices can be recognized and...