Elasticity of Crystalline ß-Sheet Monolayers.

Designed amphiphilic β-sheet peptides with the sequence ProGlu(PheGlu)Pro (n = 2–7) were previously shown by grazing incidence X-ray diffraction (GIXD), to form ordered two-dimensional (2-D) monolayer structures at interfaces induced by the proline residues at peptide termini. The GIXD diffracti...

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Bibliographic Details

Published in:	Journal of the American Chemical Society Vol. 128; no. 38; pp. 12468 - 12473
Main Authors:	Isenberg, Hila, Kjaer, Kristian, Rapaport, Hanna
Format:	Article
Published:	American Chemical Society 9/27/2006
Subjects:	Peptides Optical diffraction Heme Proteins Hydrostatics Organic acids
Online Access:	View this record in EBSCOhost