Premium
Presence of pseudo‐peptide bond in the crystal structure of n‐(t‐butoxycarbonyl)‐ε‐n′‐benzyloxycarbony‐l‐lysyl‐l‐isoleucine (boc‐lys(obzl)‐ile)
Author(s) -
Malathy Sony S. M.,
Sukumar N.,
Ponnuswamy M. N.,
Jayakumar R.
Publication year - 2004
Publication title -
crystal research and technology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.377
H-Index - 64
eISSN - 1521-4079
pISSN - 0232-1300
DOI - 10.1002/crat.200310197
Subject(s) - chemistry , monoclinic crystal system , hydrogen bond , dipeptide , molecule , peptide , stereochemistry , crystallography , crystal structure , peptide bond , side chain , polymer , organic chemistry , biochemistry
The dipeptide Boc‐Lys(OBzl)‐Ile crystallizes in monoclinic space group P2 1 with cell parameters a = 5.003(1), b = 19.199(3), c = 15.270(2)Å, β =93.42(1)°, V = 1464.1(3)Å 3 , Z = 2, D cal = 1.117 Mg/m 3 at T = 293 K. The structure was solved by direct methods and refined by full‐matrix least‐squares procedure to a final R = 0.096 and wR = 0.101 using 1379 reflections. The peptide unit is in trans conformation and the molecule takes up an extended conformation. In the lysine side chain, delocalization of electrons and pseudo peptide bond formation is observed at the interaction site of benzyloxycarbonyl group. Both N‐H…O and main chain C‐H…O hydrogen bonds stabilize the molecules in the unit cell in a parallel β‐sheet fashion. (© 2004 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim)