期刊
STRUCTURE
卷 20, 期 2, 页码 227-236出版社
CELL PRESS
DOI: 10.1016/j.str.2012.01.002
关键词
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资金
- European Community [213010, 261572]
- Centre National de la Recherche Scientifique
- Institut Pasteur
- Volkswagen Foundation
- Deutsche Forschungsgemeinschaft
- Japan Society for the Promotion of Science
- National Institute of General Medical Science's Protein Structure Initiative [U54 GM074958, U54 GM094597]
- Brussels Institute for Research and Innovation (Innoviris) [BB2B 2010-1-12]
- BBSRC [BB/J007897/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/J007897/1] Funding Source: researchfish
- Grants-in-Aid for Scientific Research [21370045] Funding Source: KAKEN
The protocols currently used for protein structure determination by nuclear magnetic resonance (NMR) depend on the determination of a large number of upper distance limits for proton-proton pairs. Typically, this task is performed manually by an experienced researcher rather than automatically by using a specific computer program. To assess whether it is indeed possible to generate in a fully automated manner NMR structures adequate for deposition in the Protein Data Bank, we gathered 10 experimental data sets with unassigned nuclear Overhauser effect spectroscopy (NOESY) peak lists for various proteins of unknown structure, computed structures for each of them using different, fully automatic programs, and compared the results to each other and to the manually solved reference structures that were not available at the time the data were provided. This constitutes a stringent blind assessment similar to the CASP and CAPRI initiatives. This study demonstrates the feasibility of routine, fully automated protein structure determination by NMR.
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