title: The conformational locking of asparagine.
abstract: One dominant structure has been identified analysing the rotational spectrum of asparagine in sharp contrast with the multiconformational behaviour for other amino acids with polar side chains. This locking of the conformational variety to a single conformer has been ascribed to an intramolecular hydrogen bonding network involving α-amine, α-carboxylic and amide groups.
authors.affiliation: Grupo de Espectroscopía Molecular, Edificio Quifima, Área de Química-Física, Laboratorios de Espectroscopia y Bioespectroscopia, Parque Científico UVa, Universidad de Valladolid, 47005 Valladolid, Spain.
authors.forename: Carlos
authors.initials: C
authors.lastname: Cabezas
authors.forename: Marcelino
authors.initials: M
authors.lastname: Varela
authors.forename: Isabel
authors.initials: I
authors.lastname: Peña
authors.forename: Santiago
authors.initials: S
authors.lastname: Mata
authors.forename: Juan C
authors.initials: JC
authors.lastname: López
authors.forename: José L
authors.initials: JL
authors.lastname: Alonso
mesh_terms: D001216:Asparagine / Q000737:chemistry*; D005583:Fourier Analysis; D006860:Hydrogen Bonding; D007834:Lasers; D008872:Microwaves; D008968:Molecular Conformation; D013057:Spectrum Analysis / Q000379:methods
chemical_list: D001216:Asparagine