Peptoid residues and beta-turn formation.
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.
Rainaldi
Mario
M
Biopolymer Research Centre, CNR, Department of Organic Chemistry, University of Padova, Italy.
Moretto
Vitrorio
V
Crisma
Marco
M
Peggion
Evaristo
E
Mammi
Stefano
S
Toniolo
Claudio
C
Cavicchioni
Giorgio
G
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
C119042:N-isobutylglycine; D034444:Peptoids; D020033:Protein Isoforms; D002725:Chloroform; D005998:Glycine; D012521:Sarcosine