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.
Tremmel
Peter
P
Institut für Organische Chemie, Fakultät für Chemie und Pharmazie, Universität Regensburg, Universitätsstrasse 31, 93040 Regensburg, Germany.
Geyer
Armin
A
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