Home Study on β-sheet packing, stabilized by aromatic interactions in a tri-peptide crystal
Article
Licensed
Unlicensed Requires Authentication

Study on β-sheet packing, stabilized by aromatic interactions in a tri-peptide crystal

  • Ravindranath S. Rathore
Published/Copyright: September 25, 2009

Abstract

The role of unconventional aromatic interactions in the β-sheet packing, inside the crystal, has been highlighted. Crystal structure of terminally blocked tri-peptide, Z-L-Ala-L-Ala-L-Leu-pNA has been determined. There are four different conformers of tri-peptide inside the unit-cell, in space group P1. All the four independent molecules are described by semi-extended backbone conformations which form an anti-parallel β-sheet. The inter β-sheet packing is predominantly stabilized by C—H…π and ππ interactions. In ππ interactions, the center-to-center distance between aromatic rings varies from 3.8 Å to 4.6 Å while the closest distance of approach ranges from 3.4 Å to 3.8 Å. The associations of aromatic-aromatic rings are described by either face-to-face or inclined arrangements.

:
Published Online: 2009-9-25
Published in Print: 2004-9-1

© 2004 Oldenbourg Wissenschaftsverlag GmbH

Downloaded on 13.10.2025 from https://www.degruyterbrill.com/document/doi/10.1524/zkri.219.9.567.44043/html
Scroll to top button