期刊
COMMUNICATIONS BIOLOGY
卷 5, 期 1, 页码 -出版社
NATURE PORTFOLIO
DOI: 10.1038/s42003-022-03411-y
关键词
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资金
- National Institute of General Medical Sciences [R01GM127267]
- Glycoscience Center of Research Excellence [NIH P20GM130460, R01GM134335]
- NIH [P41GM111135]
- NSF [CHE 1750666]
This study presents a mass spectrometry-based method that guides computational modeling for de novo protein structure prediction. The method was successfully used to determine the structure of a protein with no close homolog of known structure.
A mass spectrometry-based method guides computational modeling for de novo protein structure prediction. High resolution hydroxyl radical protein footprinting (HR-HRPF) is a mass spectrometry-based method that measures the solvent exposure of multiple amino acids in a single experiment, offering constraints for experimentally informed computational modeling. HR-HRPF-based modeling has previously been used to accurately model the structure of proteins of known structure, but the technique has never been used to determine the structure of a protein of unknown structure. Here, we present the use of HR-HRPF-based modeling to determine the structure of the Ig-like domain of NRG1, a protein with no close homolog of known structure. Independent determination of the protein structure by both HR-HRPF-based modeling and heteronuclear NMR was carried out, with results compared only after both processes were complete. The HR-HRPF-based model was highly similar to the lowest energy NMR model, with a backbone RMSD of 1.6 angstrom. To our knowledge, this is the first use of HR-HRPF-based modeling to determine a previously uncharacterized protein structure.
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