A β/γ Motif to Mimic α‐Helical Turns in Proteins

Abstract

The combination of the properties of β- and γ-amino acids produce extended artificial fragments that recreate the properties of a natural α-helix. The substitution of two α-helical turns in an otherwise natural coiled-coil motif by a fragment of alternating β- and γ-amino acids with retention of global conformation and stability of the fold was established. The new chimeric system shows a high potency in helical quaternary structure formation. 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.