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Charge‐Based Interactions between Peptides Observed as the Dominant Force for Association in Aqueous Solution
Author(s) -
McLain Sylvia E.,
Soper Alan K.,
Daidone Isabella,
Smith Jeremy C.,
Watts Anthony
Publication year - 2008
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200802679
Subject(s) - aqueous solution , peptide , neutron diffraction , molecule , charge (physics) , alanine , chemical physics , snapshot (computer storage) , chemistry , diffraction , association (psychology) , crystallography , materials science , physics , computer science , amino acid , optics , organic chemistry , biochemistry , crystal structure , quantum mechanics , psychology , psychotherapist , operating system
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.)
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