A new motif in the formation of peptide nanotubes: the crystallographic signatureRay, S., Haldar, D., Drew, M.G.B. and Banerjee, A. (2004) A new motif in the formation of peptide nanotubes: the crystallographic signature. Organic Letters, 6 (24). pp. 4463-4465. 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/ol048253a Abstract/SummaryTerminally protected acyclic tripeptides Boc-Tyr(1)-Val(2)-Tyr(3)-OMe 1 and Boc-Tyr(1)-lle(2)-Tyr(3)-OMe 2 self-assemble into nanotubes in crystals through various noncovalent interactions with an average internal diameter of 5 Angstrom (0.5 nm), and the tubular ensemble is developed through the hydrogen-bonded side chains of tyrosine residues. The inside of the hollow nanotubular structures is hydrophilic; however, no solvent molecules have been crystallographically detected.
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