Homology modeling of larger proteins guided by chemical shifts.
basic_science · Level V
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- Record sourced from PubMed, PMID 26053889.
- Also identified by DOI 10.1038/nmeth.3437 and PMC identifier 4521993.
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Abstract
We describe an approach to the structure determination of large proteins that relies on experimental NMR chemical shifts, plus sparse nuclear Overhauser effect (NOE) data if available. Our alignment method, POMONA (protein alignments obtained by matching of NMR assignments), directly exploits pre-existing bioinformatics algorithms to match experimental chemical shifts to values predicted for the crystallographic database. Protein templates generated by POMONA are subsequently used as input for chemical shift-based Rosetta comparative modeling (CS-RosettaCM) to generate reliable full-atom models.
Medical subject headings
- Computational Biology
- Magnetic Resonance Spectroscopy
- Proteins