Protein α‐Turns Recreated in Structurally Stable Small Molecules

Abstract

α-Turn mimics: α-Turns in proteins vary in three sets of (ϕ, ψ) angles that determine peptide backbone shape and helical pitch. Structures of cyclic tetrapeptides 1 and 2 are shown to closely match two α-turn types that are structurally influential at key sites in 20 proteins described. NMR and CD spectroscopy as well as MD simulations have been used to characterize these first examples of non-helical α-turns created in small molecules. Detailed facts of importance to specialist readers are published as ”Supporting Information”. Such documents are peer-reviewed, but not copy-edited or typeset. They are made available as submitted by the authors. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.