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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

Abstract

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
OAI identifier: oai:CiteSeerX.psu:10.1.1.135.942
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