Görbitz Carl Henrik, Bruvoll Marius, Dizdarevic Selma, Fimland Nina, Hafizovic Jasmina, Kalfjøs Helen Therese, Krivokapic Alexander, Vestli Kristian
Department of Chemistry, University of Oslo, PO Box 1033, Blindern, N-0315 Oslo, Norway.
Acta Crystallogr C. 2006 Jan;62(Pt 1):o22-5. doi: 10.1107/S0108270105038928. Epub 2005 Dec 16.
The structures of the title dipeptides, C9H18N2O4.0.33H2O, C12H16N2O4 and C8H16N2O4S.0.34H2O, complete a series of investigations focused on L-Xaa-L-serine peptides, where Xaa is a hydrophobic residue. All three structures are divided into hydrophilic and hydrophobic layers. The hydrophilic layers are thin for L-phenylalanyl-L-serine, rendered possible by an unusual peptide conformation, and thick for L-isoleucyl-L-serine and L-methionyl-L-serine, which include cocrystallized water molecules on the twofold axes.