We thank Leighton Coates (Oak Ridge National Laboratory) and Thomas Splettstoesser (University of Heidelberg) for help with graphical representations and Christopher Stanley (Oak Ridge National Laboratory) for useful discussions. JCS was funded by Laboratory Research and Development funds provided by the US Department of Energy.
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Communication
Charge-Based Interactions between Peptides Observed as the Dominant Force for Association in Aqueous Solution†
Article first published online: 20 OCT 2008
DOI: 10.1002/anie.200802679
Copyright © 2008 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Issue
Angewandte Chemie International Edition
Volume 47, Issue 47, pages 9059–9062, November 10, 2008
Additional Information
How to Cite
McLain, Sylvia E., Soper, Alan K., Daidone, I., Smith, Jeremy C. and Watts, A. (2008), Charge-Based Interactions between Peptides Observed as the Dominant Force for Association in Aqueous Solution. Angew. Chem. Int. Ed., 47: 9059–9062. doi: 10.1002/anie.200802679
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Publication History
- Issue published online: 5 NOV 2008
- Article first published online: 20 OCT 2008
- Manuscript Revised: 11 AUG 2008
- Manuscript Received: 6 JUN 2008
Keywords:
- charge–charge interactions;
- hydrophobic effects;
- molecular dynamics;
- neutron diffraction;
- peptide association
What's the attraction? The structures of three dipeptides in aqueous solutions were investigated by using a combination of neutron diffraction and computer simulation. In each solution, peptide association was dominated by charge–charge rather than hydrophobic interactions (see the representative snapshot of the peptide/water box for glycyl-L-alanine; the water molecules are depicted by red crosses.)