Work

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

Year: 1987

Type: article

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.

Source: FEBS Letters

DOI: 10.1016/0014-5793(87)80201-6

Authors: Walter J. Chazin, Mark Rance, Peter E. Wright

Institutions: Scripps Research Institute, Scripps Clinic

Language: English

Topic: Advanced NMR Techniques and Applications

Subfield: Spectroscopy

Field: Chemistry

Domain: Physical Sciences

Open Access status: bronze

Funders: National Science Foundation, National Institutes of Health, National Institute of General Medical Sciences

Awards: G3119572438, Applications of Multiple Quantum Techniques in Protein NMR Spectroscopy