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

Academic Article
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Overview

authors

  • Chazin, Walter J.
  • Rance, M.
  • Wright, Peter

publication date

  • September 1987

journal

  • FEBS Letters  Journal

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 epsilon 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)6(3-) has been examined using this approach.

subject areas

  • Lysine
  • Magnetic Resonance Spectroscopy
  • Plastocyanin
  • Protein Conformation
  • Proteins
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Identity

International Standard Serial Number (ISSN)

  • 0014-5793

Digital Object Identifier (DOI)

  • 10.1016/0014-5793(87)80201-6

PubMed ID

  • 3115827
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Additional Document Info

start page

  • 109

end page

  • 114

volume

  • 222

issue

  • 1

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