Selective {sup 2}H and {sup 13}C labeling in NMR analysis of solution protein structure and dynamics
- Northwestern Univ., Evanston, IL (United States)
Preparation of samples bearing combined isotope enrichment patterns has played a central role in the recent advances in NMR analysis of proteins in solution. In particular, uniform {sup 13}C, {sup 15}N enrichment has made it possible to apply heteronuclear multidimensional correlation experiments for the mainchain assignments of proteins larger than 30 KDa. In contrast, selective labeling approaches can offer advantages in terms of the directedness of the information provided, such as chirality and residue type assignments, as well as through enhancements in resolution and sensitivity that result from editing the spectral complexity, the relaxation pathways and the scalar coupling networks. In addition, the combination of selective {sup 13}C and {sup 2}H enrichment can greatly facilitate the determination of heteronuclear relaxation behavior.
- Research Organization:
- Los Alamos National Lab. (LANL), Los Alamos, NM (United States)
- OSTI ID:
- 83380
- Report Number(s):
- LA-12893-C; CONF-9403228-; ON: DE95012795; TRN: 95:004732-0011
- Resource Relation:
- Conference: Stable isotope applications in biomolecular structure and mechanisms, Santa Fe, NM (United States), 27-31 Mar 1994; Other Information: PBD: Dec 1994; Related Information: Is Part Of Stable isotope applications in biomolecular structure and mechanisms. A meeting to bring together producers and users of stable-isotope-labeled compounds to assess current and future needs; Trewhella, J.; Cross, T.A.; Unkefer, C.J. [eds.]; PB: 382 p.
- Country of Publication:
- United States
- Language:
- English
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