title: What are the preferred horizontal displacements of aromatic-aromatic interactions in proteins? Comparison with the calculated benzene-benzene potential energy surface.
abstract: The data from protein structures from the Protein Data Bank and quantum chemical calculations indicate the importance of aromatic-aromatic interactions at large horizontal displacements (offsets). The protein stacking interactions of the phenylalanine residue show preference for large offsets (3.5-5.0 Å), while the calculations show substantially strong interactions, of about -2.0 kcal mol(-1).
authors.affiliation: Innovation center of the Department of Chemistry, Studentski trg 12-16, 11000 Belgrade, Serbia.
authors.forename: Dragan B
authors.initials: DB
authors.lastname: Ninković
authors.forename: Jelena M
authors.initials: JM
authors.lastname: Andrić
authors.forename: Saša N
authors.initials: SN
authors.lastname: Malkov
authors.forename: Snežana D
authors.initials: SD
authors.lastname: Zarić
mesh_terms: D001554:Benzene / Q000737:chemistry*; D030562:Databases, Protein; D010649:Phenylalanine / Q000737:chemistry; D011506:Proteins / Q000737:chemistry*; D011789:Quantum Theory; D013499:Surface Properties
chemical_list: D011506:Proteins; D010649:Phenylalanine; D001554:Benzene