Issue 14, 2005

X-Ray crystallographic signature of supramolecular triple helix formation from a water soluble synthetic tetrapeptide

Abstract

Single crystal X-ray diffraction studies on the water soluble, synthetic tetrapeptide Tyr(1)–Aib(2)–Tyr(3)–Val(4) 1 with a non-coded amino acid residue (Aib: α-amino isobutyric acid) reveal that the peptide adopts an “S”-shaped molecular structure which self-assembles to form a supramolecular triple helix using various non-covalent interactions including water mediated hydrogen bonds in the solid state.

Graphical abstract: X-Ray crystallographic signature of supramolecular triple helix formation from a water soluble synthetic tetrapeptide

Supplementary files

Article information

Article type
Communication
Submitted
25 Nov 2004
Accepted
03 Feb 2005
First published
16 Feb 2005

Chem. Commun., 2005, 1836-1838

X-Ray crystallographic signature of supramolecular triple helix formation from a water soluble synthetic tetrapeptide

A. K. Das, D. Haldar, R. P. Hegde, N. Shamala and A. Banerjee, Chem. Commun., 2005, 1836 DOI: 10.1039/B417726F

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