Presence of pseudo-peptide bond in the crystal structure of n-(t-butoxycarbonyl)-ε-n′-benzyloxycarbony-l-lysyl-l-isoleucine (boc-lys(obzl)-ile)

The dipeptide Boc‐Lys(OBzl)‐Ile crystallizes in monoclinic space group P21 with cell parameters a = 5.003(1), b = 19.199(3), c = 15.270(2)Å, β =93.42(1)°, V = 1464.1(3)Å3, Z = 2, Dcal = 1.117 Mg/m3 at T = 293 K. The structure was solved by direct methods and refined by full‐matrix least‐squares proc...

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Bibliographic Details
Published in:Crystal research and technology (1979) 2004-04, Vol.39 (4), p.368-374
Main Authors: Malathy Sony, S. M., Sukumar, N., Ponnuswamy, M. N., Jayakumar, R.
Format: Article
Language:English
Subjects:
crystal
dipeptide
hydrogen bonds
isoleucine
lysine
pseudo peptide bond
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Summary:The dipeptide Boc‐Lys(OBzl)‐Ile crystallizes in monoclinic space group P21 with cell parameters a = 5.003(1), b = 19.199(3), c = 15.270(2)Å, β =93.42(1)°, V = 1464.1(3)Å3, Z = 2, Dcal = 1.117 Mg/m3 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)
ISSN:0232-1300
1521-4079
DOI:10.1002/crat.200310197