Isotope labeling for NMR studies of macromolecular structure and interactions
- Scripps Research Institute, La Jolla, CA (United States)
Implementation of biosynthetic methods for uniform or specific isotope labeling of proteins, coupled with the recent development of powerful heteronuclear multidimensional NMR methods, has led to a dramatic increase in the size and complexity of macromolecular systems that are now amenable to NMR structural analysis. In recent years, a new technology has emerged that combines uniform {sup 13}C, {sup 15}N labeling with heteronuclear multidimensional NMR methods to allow NMR structural studies of systems approaching 25 to 30 kDa in molecular weight. In addition, with the introduction of specific {sup 13}C and {sup 15}N labels into ligands, meaningful NMR studies of complexes of even higher molecular weight have become feasible. These advances usher in a new era in which the earlier, rather stringent molecular weight limitations have been greatly surpassed and NMR can begin to address many central biological problems that involve macromolecular structure, dynamics, and interactions.
- Research Organization:
- Los Alamos National Lab., NM (United States)
- OSTI ID:
- 83371
- Report Number(s):
- LA--12893-C; CONF-9403228--; ON: DE95012795; CNN: Grant GM36643; Grant CA27498
- Country of Publication:
- United States
- Language:
- English
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