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Homology modeling of larger proteins guided by chemical shifts.

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.

SUBMITTER: Shen Y

PROVIDER: S-EPMC4521993 | biostudies-literature | 2015 Aug

REPOSITORIES: biostudies-literature

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Homology modeling of larger proteins guided by chemical shifts.

Shen Yang Y Bax Ad A

Nature methods 20150608 8

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 c ...[more]

PMID: 26053889

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