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.
|Number of pages||6|
|Journal||International Journal of Peptide and Protein Research|
|State||Published - Oct 1983|
- X‐ray diffraction
- peptide conformation