An oligomeric ser-pro dipeptide mimetic assuming the polyproline II helix conformation.
A hexapeptide assembled from dipeptide building blocks assumes the secondary structure of the polyproline II (PPII) helix. Side chain-to-backbone hydrogen bonds stabilize peptide torsions next to the fused ring systems. The solution structure of the polyhydroxylated peptide was studied by spectroscopic methods.
Institut für Organische Chemie, Fakultät für Chemie und Pharmazie, Universität Regensburg, Universitätsstrasse 31, 93040 Regensburg, Germany.
Peter
P
Tremmel
Armin
A
Geyer
D004151:Dipeptides / Q000737:chemistry*; D007769:Lactams / Q000737:chemistry*; D008968:Molecular Conformation; D018716:Molecular Mimicry; D019906:Nuclear Magnetic Resonance, Biomolecular; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D013844:Thiazoles / Q000737:chemistry*
D004151:Dipeptides; D007769:Lactams; D010455:Peptides; D013844:Thiazoles; C011083:polyproline