Structure and conformation of n- (t-butoxycarbonyl)-l-valine- l-phenylalanine-methyl ester (Boc-Val-Phe-OMe) by A. Nallini, K. Saraboji, M. N. Ponnuswamy, and S. B. Katti

Crystal Research and Technology

Cryst. Res. Technol. 39, 179 (2004) - Abstract -

Structure and conformation of n- (t-butoxycarbonyl)-l-valine- l-phenylalanine-methyl ester (Boc-Val-Phe-OMe)

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

Department of Crystallography and Biophysics, University of Madras, Guindy Campus, Chennai –600 025, India
*Division of Biopolymers, Central Drug Research Institute, Lucknow –226 001, India

Keywords	valine, phenylalanine, peptide, crystal structure, conformation, hydrogen bonding
PACS	61.66.Hq
DOI	10.1002/crat.200310168

The crystal structure of N- (t-butoxycarbonyl) - L-valine-L-phenylalanine-methyl ester (Boc-Val-Phe-OMe), C₂₀H₃₀N₂O₅ was determined by X-ray diffraction methods. 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, V=2143.8(5)Å³, F.W.=378.46, Z=4, D_calc=1.173 Mg/m³. The structure was solved by direct methods and final R1 and wR2 are 0.0659 and 0.1654, respectively. The peptide unit is in trans conformation [ω=177.4(9)°]. The N-H…O and C-H…O hydrogen bondings influence the packing of the molecules in the dipeptide crystal.

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