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Complete assignment of lysine resonances in 1 H NMR spectra of proteins as probes of surface structure and dynamics
Author(s) -
Chazin Walter J.,
Rance Mark,
Wright Peter E.
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)80201-6
Subject(s) - lysine , spectral line , chemistry , dynamics (music) , nmr spectra database , crystallography , nuclear magnetic resonance , physics , amino acid , biochemistry , astronomy , acoustics
A strategy is presented for complete identification of 1 H 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.