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The foldamers comprise three to five monomers carrying various proteinogenic side chains, and exist as racemic mixtures of interconverting right\u2010handed and left\u2010handed helices. Functionalization of the foldamers by a nanomolar ligand of human carbonic anhydrase\u2005II (HCA) ensured that they would be held in close proximity to the protein surface. Foldamer\u2013protein interactions were screened by circular dichroism (CD). One foldamer displayed intense CD bands indicating that a preferred helix handedness is induced upon interacting with the protein surface. The crystal structure of the complex between this foldamer and HCA could be resolved at 2.1\u2005\u00c5 resolution and revealed a number of unanticipated protein\u2013foldamer, foldamer\u2013foldamer, and protein\u2013protein interactions.<\/jats:p>","DOI":"10.1002\/anie.201309160","type":"journal-article","created":{"date-parts":[[2013,11,29]],"date-time":"2013-11-29T04:37:38Z","timestamp":1385699858000},"page":"883-887","source":"Crossref","is-referenced-by-count":70,"title":["Structure of a Complex Formed by a Protein and a Helical Aromatic Oligoamide Foldamer at 2.1\u2005\u00c5 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