Complete assignment of lysine resonances in 1H NMR spectra of proteins as probes of surface structure and dynamics
- 28 September 1987
- journal article
- Published by Wiley in FEBS Letters
- Vol. 222 (1) , 109-114
- https://doi.org/10.1016/0014-5793(87)80201-6
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 Cϵ 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.Keywords
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