Restricted rotation in chiral peptide nucleic acid (PNA) monomers--influence of substituents studied by means of 1H NMR.
The influence of amino acid side chains [derived from: Ala, Val, Leu, Ile, Phe, Tyr(Bzl), Ser(Bzl), Thr(Bzl), Pro, Trp], incorporated into "aminoalkyl" part of PNA monomers, on the temperature-dependent distributions of rotamers about the tertiary amide bond was studied by means of 1H NMR at 0, 25 and 40 degrees C in CDCl3. The delta G0 values of the energy differences between individual rotamers were calculated. The results may be helpful in the designing of monomers with desirable properties.
Oleszczuk
M
M
Institute of Biochemistry and Biophysics, Polish Academy of Science, Warszawa, Poland.
Rodziewicz-Motowidlo
S
S
Falkiewicz
B
B
D000596:Amino Acids / Q000737:chemistry; D019906:Nuclear Magnetic Resonance, Biomolecular; D020135:Peptide Nucleic Acids / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D011522:Protons
D000596:Amino Acids; D020135:Peptide Nucleic Acids; D010455:Peptides; D011522:Protons