A new molecular scaffold for the formation of supramolecular peptide double helices: the crystallographic insightGuha, S., Drew, M.G.B. and Banerjee, A. (2007) A new molecular scaffold for the formation of supramolecular peptide double helices: the crystallographic insight. Organic Letters, 9 (7). pp. 1347-1350. ISSN 1523-7060 Full text not archived in this repository. It is advisable to refer to the publisher's version if you intend to cite from this work. See Guidance on citing. To link to this item DOI: 10.1021/ol0701870 Abstract/SummaryA series of water-soluble synthetic dipeptides (1-3) with an N-terminally located beta-alanine residue, beta-alanyl-L-valine (1), beta-alanyl-L-isoleucine (2), and beta-alanyl-L-phenylalanine (3, form hydrogen-bonded supramolecular double helices with a pitch length of 1 nm, whereas the C-terminally positioned beta-alanine containing dipeptide (4), L-phenylalanyl-beta-alanine, does not form a supramolecular double helical structure. beta-Ala-Xaa (Xaa = Val/Ile/Phe) can be regarded as a new motif for the formation of supramolecular double helical structures in the solid state.
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