title: Peptoid residues and beta-turn formation.
abstract: A set of terminally protected tripeptoids containing a residue of either N-methylglycine or N-isobutylglycine in position i + 1/i + 2 were synthesized and tested for intramolecularly H-bonded beta-turn formation. By exploiting FT-IR absorption and 1H NMR techniques, their folding tendencies were compared with those of a variety of reference peptides. The amount of beta-turn induction and the relative extent of the various types of intramolecularly H-bonded beta-turn conformers were determined in chloroform solution.
authors.affiliation: Biopolymer Research Centre, CNR, Department of Organic Chemistry, University of Padova, Italy.
authors.forename: Mario
authors.initials: M
authors.lastname: Rainaldi
authors.forename: Vitrorio
authors.initials: V
authors.lastname: Moretto
authors.forename: Marco
authors.initials: M
authors.lastname: Crisma
authors.forename: Evaristo
authors.initials: E
authors.lastname: Peggion
authors.forename: Stefano
authors.initials: S
authors.lastname: Mammi
authors.forename: Claudio
authors.initials: C
authors.lastname: Toniolo
authors.forename: Giorgio
authors.initials: G
authors.lastname: Cavicchioni
mesh_terms: D000595:Amino Acid Sequence; D002725:Chloroform / Q000737:chemistry; D005998:Glycine / Q000031:analogs & derivatives* / Q000737:chemistry; D006860:Hydrogen Bonding; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods; D034444:Peptoids / Q000031:analogs & derivatives* / Q000138:chemical synthesis / Q000737:chemistry; D020033:Protein Isoforms; D017433:Protein Structure, Secondary; D012521:Sarcosine / Q000737:chemistry; D017550:Spectroscopy, Fourier Transform Infrared
chemical_list: C119042:N-isobutylglycine; D034444:Peptoids; D020033:Protein Isoforms; D002725:Chloroform; D005998:Glycine; D012521:Sarcosine