Unconstrained Homooligomeric γ‑Peptides Show High Propensity for C₁₄ Helix Formation

Abstract

Monosubstituted γ⁴-residues (γ⁴Leu, γ⁴Ile, and γ⁴Val) form helices even in short homooligomeric sequences. C₁₄ helix formation is established by X-ray diffraction in homooligomeric (γ)_<i>n</i> tetra-, hexa- and decapeptide sequences demonstrating the high propensity of γ residues, with proteinogenic side chains, to adopt locally folded conformations