Racemic dipeptide glycyl-DL-leucine at 120 K.

P. Bombicz, B. Dittrich, M. Strumpel, H. P. Nabein, P. Luger

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

The structure of glycyl-DL-leucine, C(8)H(16)N(2)O(3), has been determined at 120 K by single-crystal X-ray diffraction. In addition to three N-H.O-type hydrogen bonds of the positively charged RNH(3)(+) group of the zwitterionic molecule, an intermolecular N-H. O contact exists between the peptide bond and the carboxylate group. Four hydrogen-bond cycles were identified, giving a complex pattern.

Original languageEnglish
JournalActa Crystallographica Section C: Crystal Structure Communications
Volume56
Publication statusPublished - Dec 2000

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leucine
Dipeptides
Leucine
Hydrogen
Hydrogen bonds
hydrogen bonds
X-Ray Diffraction
carboxylates
peptides
Single crystals
X ray diffraction
Peptides
cycles
Molecules
single crystals
diffraction
molecules
x rays

ASJC Scopus subject areas

  • Condensed Matter Physics
  • Structural Biology

Cite this

Racemic dipeptide glycyl-DL-leucine at 120 K. / Bombicz, P.; Dittrich, B.; Strumpel, M.; Nabein, H. P.; Luger, P.

In: Acta Crystallographica Section C: Crystal Structure Communications, Vol. 56, 12.2000.

Research output: Contribution to journalArticle

Bombicz, P. ; Dittrich, B. ; Strumpel, M. ; Nabein, H. P. ; Luger, P. / Racemic dipeptide glycyl-DL-leucine at 120 K. In: Acta Crystallographica Section C: Crystal Structure Communications. 2000 ; Vol. 56.
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