TY - JOUR
T1 - Crystal structure of L‐lysyl‐L‐glutamic acid dihydrate
AU - YENNAWAR, HEMANT P.
AU - VISWAMITRA, M. A.
PY - 1989/7
Y1 - 1989/7
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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U2 - 10.1111/j.1399-3011.1989.tb01006.x
DO - 10.1111/j.1399-3011.1989.tb01006.x
M3 - Article
AN - SCOPUS:85004805860
SN - 0367-8377
VL - 34
SP - 42
EP - 45
JO - International Journal of Peptide and Protein Research
JF - International Journal of Peptide and Protein Research
IS - 1
ER -