Crystal structure of L‐lysyl‐L‐glutamic acid dihydrate

Hemant P. Yennawar, M. A. VISWAMITRA

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

L‐Lysyl‐L‐glutamic acid dihydrate, C11N3O5H21·2H2O, crystallizes in the monoclinic space group P21 with a = 12.474(2), b = 5.020(1), c = 13.157(2) Å, β= 114.69(1)° and Z = 2. The crystal structure was solved by direct methods and refined to an R value of 0.037 using full matrix least‐squares method. The molecule exists as a double zwitterion with both the amino and carboxyl groups ionised. The peptide has a folded conformation with its Lys residue trans and Glu residue gauchegauche+. The side chains of the Lys and Glu residues correspond to all trans and folded (ggg) conformations respectively. The terminal carboxyl group forms hydrogen bonds with the ξ‐amino group of the lysine side chain. The head‐to‐tail interaction often seen in peptide crystals is absent in the present structure. In the extended crystal structure water molecules form channels along the b direction and are enclosed within helically arranged hydrogen bonds formed by the lysine side chain and the peptide backbone.

Original languageEnglish (US)
Pages (from-to)42-45
Number of pages4
JournalInternational Journal of Peptide and Protein Research
Volume34
Issue number1
DOIs
StatePublished - Jan 1 1989

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Crystal structure
Peptides
Lysine
Acids
Conformations
Hydrogen
Hydrogen bonds
Molecules
Crystals
Water
Direction compound

All Science Journal Classification (ASJC) codes

  • Biochemistry

Cite this

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title = "Crystal structure of L‐lysyl‐L‐glutamic acid dihydrate",
abstract = "L‐Lysyl‐L‐glutamic acid dihydrate, C11N3O5H21·2H2O, crystallizes in the monoclinic space group P21 with a = 12.474(2), b = 5.020(1), c = 13.157(2) {\AA}, β= 114.69(1)° and Z = 2. The crystal structure was solved by direct methods and refined to an R value of 0.037 using full matrix least‐squares method. The molecule exists as a double zwitterion with both the amino and carboxyl groups ionised. The peptide has a folded conformation with its Lys residue trans and Glu residue gauche−gauche+. The side chains of the Lys and Glu residues correspond to all trans and folded (g−g−g−) conformations respectively. The terminal carboxyl group forms hydrogen bonds with the ξ‐amino group of the lysine side chain. The head‐to‐tail interaction often seen in peptide crystals is absent in the present structure. In the extended crystal structure water molecules form channels along the b direction and are enclosed within helically arranged hydrogen bonds formed by the lysine side chain and the peptide backbone.",
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Crystal structure of L‐lysyl‐L‐glutamic acid dihydrate. / Yennawar, Hemant P.; VISWAMITRA, M. A.

In: International Journal of Peptide and Protein Research, Vol. 34, No. 1, 01.01.1989, p. 42-45.

Research output: Contribution to journalArticle

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AU - VISWAMITRA, M. A.

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Y1 - 1989/1/1

N2 - L‐Lysyl‐L‐glutamic acid dihydrate, C11N3O5H21·2H2O, crystallizes in the monoclinic space group P21 with a = 12.474(2), b = 5.020(1), c = 13.157(2) Å, β= 114.69(1)° and Z = 2. The crystal structure was solved by direct methods and refined to an R value of 0.037 using full matrix least‐squares method. The molecule exists as a double zwitterion with both the amino and carboxyl groups ionised. The peptide has a folded conformation with its Lys residue trans and Glu residue gauche−gauche+. The side chains of the Lys and Glu residues correspond to all trans and folded (g−g−g−) conformations respectively. The terminal carboxyl group forms hydrogen bonds with the ξ‐amino group of the lysine side chain. The head‐to‐tail interaction often seen in peptide crystals is absent in the present structure. In the extended crystal structure water molecules form channels along the b direction and are enclosed within helically arranged hydrogen bonds formed by the lysine side chain and the peptide backbone.

AB - L‐Lysyl‐L‐glutamic acid dihydrate, C11N3O5H21·2H2O, crystallizes in the monoclinic space group P21 with a = 12.474(2), b = 5.020(1), c = 13.157(2) Å, β= 114.69(1)° and Z = 2. The crystal structure was solved by direct methods and refined to an R value of 0.037 using full matrix least‐squares method. The molecule exists as a double zwitterion with both the amino and carboxyl groups ionised. The peptide has a folded conformation with its Lys residue trans and Glu residue gauche−gauche+. The side chains of the Lys and Glu residues correspond to all trans and folded (g−g−g−) conformations respectively. The terminal carboxyl group forms hydrogen bonds with the ξ‐amino group of the lysine side chain. The head‐to‐tail interaction often seen in peptide crystals is absent in the present structure. In the extended crystal structure water molecules form channels along the b direction and are enclosed within helically arranged hydrogen bonds formed by the lysine side chain and the peptide backbone.

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