Structures of Larger Proteins in Solution: Three- and Four-Dimensional Heteronuclear NMR Spectroscopy
Abstract
Three- and four-dimensional heteronuclear nuclear magnetic resonance (NM_R) spectroscopy offers dramatic improvements in spectral resolution by spreading throughbond and through-space correlations in three and four orthogonal frequency axes. Simultaneously, large beteronuclear couplings are exploited to circumvent problems due to the larger linewidths that are associated with increasing molecular weight. These novel experiments have been designed to extend the application of NMR as a method for determining three-dimensional structures of proteins in solution beyond the limits of conventional two-dimensional NMR (≈100 residues) to molecules in the 150- to 300-residue range. This potential has recently been confirmed with the determination of the highresolution NMR structure of a protein greater than 150 residues, namely, interleukin-1β.
- Publication:
-
Science
- Pub Date:
- June 1991
- DOI:
- 10.1126/science.252.5011.1390
- Bibcode:
- 1991Sci...252.1390M