ja993609c_si_001.pdf (62.68 kB)
Large Variations in One-Bond 13Cα−13Cβ J Couplings in Polypeptides Correlate with Backbone Conformation
journal contribution
posted on 2000-02-23, 00:00 authored by Gabriel Cornilescu, Ad Bax, David A. CaseOne-bond 1JCαCβ scalar couplings, measured in the protein ubiquitin, exhibit a strong dependence
on the local backbone conformation. Empirically, the deviation from the 1JCαCβ value measured in the
corresponding free amino acid, can be expressed as Δ1JCαCβ = 1.3 + 0.6 cos(ψ − 61°) + 2.2 cos[2(ψ − 61°)]
− 0.9 cos[2(φ + 20°)] ± 0.5 Hz, where φ and ψ are the intraresidue polypeptide backbone torsion angles
obtained from ubiquitin's X-ray structure. The relation between 1JCαCβ and backbone torsion angles is confirmed
by density functional theory (DFT) calculations on the peptide analogue Ace-Ala-NMe.