Novel conformationally-constrained beta-peptides characterized by 1H NMR chemical shifts.
For a novel family of oxanorbornene beta-peptides, density functional theory computations of the three-dimensional structure and 1H NMR chemical shifts predict that the dimer and trimer form consecutive 8-membered hydrogen-bonded ring helices, which is supported by excellent agreement with experimental solution NMR data.
Department of Chemistry, University of Pennsylvania, 231 S. 34th Street, Philadelphia, PA 19104-6323, USA.
Robert J
RJ
Doerksen
Bin
B
Chen
Jing
J
Yuan
Jeffrey D
JD
Winkler
Michael L
ML
Klein
D001643:Bridged Bicyclo Compounds / Q000737:chemistry; D019281:Dimerization; D006860:Hydrogen Bonding; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D010456:Peptides, Cyclic / Q000737:chemistry*; D017433:Protein Structure, Secondary; D013816:Thermodynamics
D001643:Bridged Bicyclo Compounds; D010456:Peptides, Cyclic