title: What are preferred water-aromatic interactions in proteins and crystal structures of small molecules?
abstract: The distribution of water molecules around aromatic rings in the protein structures and crystal structures of small molecules shows quite a small number of the strongest OH-π interactions, a larger number of parallel interactions, and the largest number of the weakest CH-O interactions.
authors.affiliation: Institute of Chemistry, Technology and Metallurgy, University of Belgrade, Njegoševa 12, P.O. Box 473, Belgrade, Serbia.
authors.forename: Goran V
authors.initials: GV
authors.lastname: Janjić
authors.forename: Saša N
authors.initials: SN
authors.lastname: Malkov
authors.forename: Miodrag V
authors.initials: MV
authors.lastname: Zivković
authors.forename: Snežana D
authors.initials: SD
authors.lastname: Zarić
mesh_terms: D018360:Crystallography, X-Ray; D006860:Hydrogen Bonding; D008968:Molecular Conformation; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism; D011726:Pyridinium Compounds / Q000737:chemistry; D014867:Water / Q000737:chemistry*
chemical_list: D011506:Proteins; D011726:Pyridinium Compounds; D014867:Water