JOURNAL ARTICLE

L-Isoleucyl-L-serine 0.33-hydrate,L-phenylalanyl-L-serine andL-methionyl-L-serine 0.34-hydrate

Carl Henrik GörbitzM. BruvollS. DizdarevicN. FimlandJ. HafizovicH.T. KalfjosAlexander KrivokapićKristian Vestli

Year: 2005 Journal:   Acta Crystallographica Section C Crystal Structure Communications Vol: 62 (1)Pages: o22-o25   Publisher: Wiley

Abstract

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.

Keywords:
Serine Chemistry Peptide Stereochemistry Biochemistry Phosphorylation

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Citation History

Topics

Supramolecular Self-Assembly in Materials
Physical Sciences →  Materials Science →  Biomaterials
Chemical Synthesis and Analysis
Life Sciences →  Biochemistry, Genetics and Molecular Biology →  Molecular Biology
Enzyme Structure and Function
Physical Sciences →  Materials Science →  Materials Chemistry

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