Guha, Samit ; Drew, Michael G. B. ; Banerjee, Arindam (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 available from this repository.
Official URL: http://pubs.acs.org/doi/abs/10.1021/ol0701870
Related URL: http://dx.doi.org/10.1021/ol0701870
Abstract
A series of water-soluble synthetic dipeptides (1−3) with an N-terminally located β-alanine residue, β-alanyl-l-valine (1), β-alanyl-l-isoleucine (2), and β-alanyl-l-phenylalanine (3), form hydrogen-bonded supramolecular double helices with a pitch length of 1 nm, whereas the C-terminally positioned β-alanine containing dipeptide (4), l-phenylalanyl-β-alanine, does not form a supramolecular double helical structure. β-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.
| Item Type: | Article |
|---|---|
| Source: | Copyright of this article belongs to American Chemical Society. |
| ID Code: | 99584 |
| Deposited On: | 07 Nov 2016 11:27 |
| Last Modified: | 07 Nov 2016 11:27 |
Repository Staff Only: item control page
