Hydrogen bonding in solution between the uracil ring and the peptide backbone demonstrated by nuclear magnetic resonance spectroscopy.
Proton and 13C nuclear magnetic resonance measurements indicate that uracil derivatives dissolved in chloroform bind to glycine and phenylalanine tripeptide derivatives through pairs of hydrogen bonds. The N(3)--H and C(4)=0 groups of the uracil ring appear to interact with the C=0 and N--H groups, respectively, of individual amino acid residues, suggesting a fundamental complementarity between uracil and the peptide backbone. The binding occurs in the same concentration range as the hydrogen bonding between derivatives of adenine and uracil under comparable conditions.
D005998:Glycine; D006860:Hydrogen Bonding; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy; D009842:Oligopeptides; D010649:Phenylalanine; D011485:Protein Binding; D014498:Uracil
D009842:Oligopeptides; D010649:Phenylalanine; D014498:Uracil; D005998:Glycine