Crystal and molecular structure of tert. ‐butyloxycarbonyl‐L‐prolyl‐α‐aminoisobutyryl‐L‐alanyl‐α‐aminoisobutyrate methyl ester

PATRICK van ROEY, G. DAVID SMITH, T. M. BALASUBRAMANIAN, E. W. CZERWINSKI, GARLAND R. MARSHALL, F. SCOTT MATHEWS

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Abstract

Boc‐Pro‐Aib‐Ala‐Aib‐OMe crystallizes in the orthorhombic space group P21212 with cell dimensions a = 17.701 (3)Å, b = 17.476 (4)Å, c = 9.686 (2)Å, V = 2996.3 Å3. The first three residues form a single turn of a 310‐helix stabilized by two intramolecular hydrogen bonds. Comparison of the conformation of the methyl ester of the tetrapeptide with that of its benzyl ester shows differences in the individual torsion angles of up to 29°, although the overall conformation is conserved.

Original languageEnglish
Pages (from-to)404-409
Number of pages6
JournalInternational Journal of Peptide and Protein Research
Volume22
Issue number4
DOIs
StatePublished - Oct 1983

Keywords

  • 3‐helix
  • X‐ray diffraction
  • peptide conformation
  • α‐aminoisobutyrate

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