Presence of pseudo-peptide bond in the crystal structure of n-(t-butoxycarbonyl)-e-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)A, =93.42(1)DG, V = 1464.1(3)A3, 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 proce...

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Published in:Crystal research and technology (1979) 2004-04, Vol.39 (4), p.368-374
Main Authors: Sony, S M Malathy, Sukumar, N, Ponnuswamy, M N, Jayakumar, R
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container_title Crystal research and technology (1979)
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creator Sony, S M Malathy
Sukumar, N
Ponnuswamy, M N
Jayakumar, R
description 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)A, =93.42(1)DG, V = 1464.1(3)A3, 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-HO and main chain C-HO hydrogen bonds stabilize the molecules in the unit cell in a parallel -sheet fashion.
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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. 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title Presence of pseudo-peptide bond in the crystal structure of n-(t-butoxycarbonyl)-e-n'-benzyloxycarbony-l-lysyl-l-isoleucine (boc-lys(obzl)-ile)
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