Experimental charge density of an L-phenylalanine formic acid complex with a short hydrogen bond determined at 25 K

Stefan Mebs, Marc Messerschmidt, Peter Luger

Research output: Contribution to journalArticle

19 Scopus citations

Abstract

The experimental charge density and related atomic and bond topological properties of an L-phenylalanine formic acid complex were derived from a high resolution X-ray data set (sin θ/λ = 1.18 Å-1/d = 0.42 Å) measured at 25 K. The complex consists of a zwitterionic and a cationic phenylalanine molecule with formate as counterion. Special focus was directed on the density distribution in the region of a strong O-H⋯O hydrogen bond (O⋯O = 2.491(1) Å) which is formed between the two phenylalanine units. The obtained results are compared with the 15 previously derived experimental amino acid charge density data, with various theoretical calculations at experimental geometries and with the complete set of topological descriptors based on ab initio calculations of the neutral forms of all 20 amino acids published recently in the literature. A comparison of all available data in this biologically important class of compounds gives an impression about the significance of the quantitative results from experimental and theoretical charge density determinations.

Original languageEnglish (US)
Pages (from-to)656-664
Number of pages9
JournalZeitschrift fur Kristallographie
Volume221
Issue number9
DOIs
StatePublished - Sep 18 2006
Externally publishedYes

Keywords

  • Amino acids
  • Charge density
  • Short hydrogen bond
  • Single crystal structure analysis
  • X-ray diffraction

ASJC Scopus subject areas

  • Materials Science(all)
  • Condensed Matter Physics
  • Inorganic Chemistry

Fingerprint Dive into the research topics of 'Experimental charge density of an L-phenylalanine formic acid complex with a short hydrogen bond determined at 25 K'. Together they form a unique fingerprint.

  • Cite this