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Crystallization and structural studies of n-benzyloxycarbonyl-Ltyrosine-L-glycine-ethyl ester (Z-Tyr-Gly-OEt)

By A. Nallini, K. Saraboji, M. N. Ponnuswamy and S. B. Katti


It is axiomatic that efficient crystal production reflects upon the quality of structure. An empirical relation for mass proportions of two solvents in crystallization of Z-Tyr-Gly-OEt shows a linear relationship. The dipeptide crystallizes in orthorhombic space group P212121, with cell parameters a=5.0680(1)Å, b=13.8650(1)Å and c=28.2630(1)Å, Z=4, Dcalc = 1.339Mg/m 3, µ=0.820mm- 1, F000=848, CuKα = 1.5418Å. The structure was solved by direct methods and final R1 and wR2 are 0.444 and 0.1276, respectively. The structure analysis reveals the trans conformation of the peptide unit with ω=-178.2(5)˚, implying only a slight deviation from planarity. The torsion angles at glycine [φ, ψ =-84.4(7)°, 179.9(5)°] are characteristic of lefthanded poly glycine II helices. A number of N-H…O, O-H…O and C-H…O hydrogen bondings play a role in stabilizing the molecules within unit cell

Topics: Key words tyrosine, peptide, crystallization, crystal structure, conformation, hydrogen bonding. PACS 61.66.Hq
Year: 2004
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