Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 129, Issue 35, Pages 10650-+Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ja073498e
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Funding
- NCRR NIH HHS [S10RR023677] Funding Source: Medline
- NIBIB NIH HHS [P41EB002031] Funding Source: Medline
- NIGMS NIH HHS [R01GM73770] Funding Source: Medline
- PHS HHS [P20-17716] Funding Source: Medline
- Div Of Molecular and Cellular Bioscience
- Direct For Biological Sciences [0815865] Funding Source: National Science Foundation
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3D NCACO, NCOCA, and CANCO scalar-coupling driven correlation experiments are presented for protein backbone assignments in the solid-state. These I -MAS experiments show superior resolution in the indirect dimensions through the elimination of heteronuclear and homonuclear couplings and enhanced sensitivity, which allow us to trace out the entire protein backbone for G131. Our results demonstrate that scalar-based methods are sufficiently well-developed to serve as a complementary tool to dipolar methods, which will be especially useful for assignment of large proteins, where resonance overlap presents a major challenge to solid-state NMR.
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