title: CH/pi interaction in the conformation of peptides. A database study.
abstract: A study was carried out, with use of the Cambridge Structural Database, to examine the role of the CH/pi interaction in the conformation of peptides. A number of short intramolecular CH/pi distances have been shown in the crystal structure of peptides bearing at least an aromatic residue in the sequence. The molecular structure in the crystal was inspected individually to know whether the conformation is merely a consequence of the so-called packing forces, or the CH/pi interaction plays a role. It has been demonstrated that the CH/pi interaction constitutes one of the key factors in controlling the conformation of peptides.
authors.affiliation: Institute of Microbial Chemistry, Tokyo, Japan.
authors.forename: Y
authors.initials: Y
authors.lastname: Umezawa
authors.forename: S
authors.initials: S
authors.lastname: Tsuboyama
authors.forename: H
authors.initials: H
authors.lastname: Takahashi
authors.forename: J
authors.initials: J
authors.lastname: Uzawa
authors.forename: M
authors.initials: M
authors.lastname: Nishio
mesh_terms: D000595:Amino Acid Sequence; D016208:Databases, Factual; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation
chemical_list: D010455:Peptides