Residue contacts predicted by evolutionary covariance extend the application of ab initio molecular replacement to larger and more challenging protein folds.
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Applications of contact predictions to structural biologyPotential DNA binding and nuclease functions of ComEC domains characterized in silico.Co-evolution techniques are reshaping the way we do structural bioinformatics.Approaches to ab initio molecular replacement of α-helical transmembrane proteins.Identification of residue pairing in interacting β-strands from a predicted residue contact map.Ensembles generated from crystal structures of single distant homologues solve challenging molecular-replacement cases in AMPLE.
P2860
Residue contacts predicted by evolutionary covariance extend the application of ab initio molecular replacement to larger and more challenging protein folds.
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2016 nî lūn-bûn
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2016 թուականի Յունիսին հրատարակուած գիտական յօդուած
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2016 թվականի հունիսին հրատարակված գիտական հոդված
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2016年の論文
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2016年論文
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2016年論文
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2016年論文
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2016年論文
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2016年論文
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2016年论文
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name
Residue contacts predicted by ...... ore challenging protein folds.
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Residue contacts predicted by ...... ore challenging protein folds.
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Residue contacts predicted by ...... ore challenging protein folds.
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Residue contacts predicted by ...... ore challenging protein folds.
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Residue contacts predicted by ...... ore challenging protein folds.
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Residue contacts predicted by ...... ore challenging protein folds.
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P2093
P2860
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Residue contacts predicted by ...... more challenging protein folds
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P2093
Jens M H Thomas
Martyn D Winn
Ronan M Keegan
P2860
P304
P356
10.1107/S2052252516008113
P577
2016-06-15T00:00:00Z