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Structure and conformation of n‐ (t‐butoxycarbonyl)‐l‐valine‐l‐phenylalanine‐methyl ester (Boc‐Val‐Phe‐OMe)
Author(s) -
Nallini A.,
Saraboji K.,
Ponnuswamy M. N.,
Katti S. B.
Publication year - 2004
Publication title -
crystal research and technology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.377
H-Index - 64
eISSN - 1521-4079
pISSN - 0232-1300
DOI - 10.1002/crat.200310168
Subject(s) - dipeptide , orthorhombic crystal system , chemistry , phenylalanine , crystal structure , stereochemistry , molecule , hydrogen bond , valine , peptide , crystallography , tripeptide , amino acid , organic chemistry , biochemistry
The crystal structure of N‐ (t‐butoxycarbonyl) ‐ L‐valine‐L‐phenylalanine‐methyl ester (Boc‐Val‐Phe‐OMe), C 20 H 30 N 2 O 5 was determined by X‐ray diffraction methods. The dipeptide crystallizes in orthorhombic space group P2 1 2 1 2 1 , with cell parameters a = 5.0680(1) Å, b = 13.8650(1) Å and c = 28.2630(1) Å, V = 2143.8(5) Å 3 , F.W. = 378.46, Z = 4, D calc = 1.173 Mg/m 3 , μ = 0.687 mm ‐1 , F 000 = 816, CuKα = 1.5418 Å. 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 conformation angles ϕ 1 , ψ 1 , ϕ 2 and ψ 2 for the peptide backbone are: ‐96.5(13)°, 101.2(13)°, ‐123.9(12)° and 34.0(15)°. The N‐H…O and C‐H…O hydrogen bondings influence the packing of the molecules in the dipeptide crystal. (© 2004 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim)