|Title||Recent developments in solid-state magic-angle spinning, nuclear magnetic resonance of fully and significantly isotopically labelled peptides and proteins|
|Publication Type||Journal Article|
|Year of Publication||2004|
|Journal||Philosophical Transactions of the Royal Society of London Series B-Biological Sciences|
|Type of Article||Review|
|Keywords||assignment strategies, CHEMICAL-SHIFT ANISOTROPIES, CROSS-POLARIZATION, DIPOLAR-CORRELATION SPECTROSCOPY, DISTANCE, HIGH-FIELD, magic-angle spinning, MAS NMR, MEASUREMENTS, MEMBRANE-PROTEIN, NMR-SPECTROSCOPY, peptide and protein labelling, RESOLUTION, ROTATING SOLIDS, SH3 DOMAIN, SOLID-STATE NMR, SPECTRIN, structural parameters|
In recent years, a large number of solid-state nuclear magnetic resonance (NMR) techniques have been developed and applied to the study of fully or significantly isotopically labelled (C-13, N-15 or C-13/N-15) biomolecules. In the past few years, the first structures of C-13/N-15-labelled peptides, Gly-Ile and Met-Leu-Phe, and a protein, Src-homology 3 domain, were solved using magic-angle spinning NMR, without recourse to any structural information obtained from other methods. This progress has been made possible by the development of NMR experiments to assign solid-state spectra and experiments to extract distance and orientational information. Another key aspect to the success of solid-state NMR is the advances made in sample preparation. These improvements will be reviewed in this contribution. Future prospects for the application of solid-state NMR to interesting biological questions will also briefly be discussed.
|URL||<Go to ISI>://000222444800010|