Complete assignment of lysine resonances in 1H NMR spectra of proteins as probes of surface structure and dynamics

Abstract

A strategy is presented for complete identification of ¹H spin systems of lysine residues using sophisticated 2D NMR experiments. Relayed and remote connectivities within each spin system are determined for spin subsystems based at the backbone amide and C^ϵ proton resonances. When complete spin system identification is combined with sequence-specific assignment, protein surface structure and dynamics can be probed in a site-specific manner. The interaction between the five lysine residues of French bean plastocyanin and a model redox partner Cr(CN)³⁻ ₆ has been examined using this approach.