title: Structure and supramolecular packing features of the dipeptide Arg-Val acetate.
abstract: The title compound crystallizes in the zwitterionic form. The crystal forms a supramolecular structure with the peptide molecules organized in head-to-tail columns in the b direction. The arginine side-chains and acetate ions interact with neighbor peptides in the c direction. Infinite hydrophobic columns are present in the a direction; they involve the valine side-chains, the acetate methyl groups and the methylene groups of the arginine side-chains. This three-dimensional organization is similar to that found in Lys-Val hydrochloride.
authors.affiliation: Departament d'Enginyeria Química, Escola Tècnica Superior d'Enginyers Industrials de Barcelona, Spain.
authors.forename: R
authors.initials: R
authors.lastname: Recacha
authors.forename: N
authors.initials: N
authors.lastname: Verdaguer
authors.forename: J A
authors.initials: JA
authors.lastname: Subirana
mesh_terms: D004151:Dipeptides / Q000737:chemistry*; D006860:Hydrogen Bonding; D008958:Models, Molecular; D011487:Protein Conformation; D014961:X-Ray Diffraction
chemical_list: D004151:Dipeptides; C110470:arginylvaline; C110469:lysylvaline