A Solid State 13C NMR, Crystallographic, and Quantum Chemical Investigation of Phenylalanine and Tyrosine Residues in Dipeptides and Proteins

We report the results of a solid-state NMR and quantum chemical investigation of the 13Cγ NMR chemical shifts in phenylalanine and tyrosine in dipeptides and proteins. Accurate computation of the experimental shifts is shown to require a good description of local electrostatic field effects, and we find the best results (R2 = 0.94, rmsd = 1.6 ppm, range = 17.1 ppm, N = 14) by using a self-consistent reaction field continuum model. There are no obvious correlations with φ, ψ, χ1, or χ2 torsion angles, unlike the results seen with other amino acids. There is, however, a linear relation between computed Cγ atomic charges and shifts for the 14 peptide as well as 18 protein residues investigated. This result is similar to the correlation reported in the 1960s between π-electron density and 13C shifts for classical 4n + 2 (n = 0, 1, 2) π-electron aromatic species, such as cyclopentadienide and the tropylium cation, and in fact, we found that the shielding/atomic charge correlation seen in the peptides and prote...