Studies on the conformation of amino acids. VI. Conformation of the proline ring as observed in crystal structures of amino acids and peptides

Abstract

The paper deals with an analysis of the available crystal structure data related to proline compounds so as to obtain information about bond lengths, bond angles, and the conformation of the pyrrolidine ring. The interesting results are: 1. The atoms Cβ, Cα, N, and Cß are nearly coplanar, with the torsion angle 0 about the Cα - N bond varying from about -15° to -15°. The Cγ atom is displaced from this plane, either up or down, so that the ring exists in one of the two puckered conformations, designated A and B. Conformation A is characterized by negative and may be termed Cγ-exo when referred to the displacement of the carbonyl carbon C. Conformation B has positive x^l and is Cγ-endo; Cγ-exo is slightly preferred over C-endo, although both conformations occur simultaneously in some crystal structures with partial probabilities. In the other structures, the non-occurring position for C^y is found to be disallowed by intermolecular contacts. The proline conformations observed correspond to the 'envelope' type of conformation of the cyclopentane ring. In peptides, the three bonds at N are nearly coplanar, and the torsion about N- Cα bond is nearly - 60°. 2. The observed ranges of (x¹, x², x³, x⁴) are (0 to –30°, 15 to 50°, –15 to - -30°, 5 to 25°) for conformation A and (20 to 35⁰, -30 to - 40⁰, 20 to 35°, 5 to -20°) for conformation B; for θ and φ the ranges are -15° to -15°, -45 to -75°. The bond lengths and bond angles are not influenced by the conformation of the ring, unlike ribose.