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Protein topology from predicted residue contacts.


ABSTRACT: Residue contacts predicted from correlated positions in a multiple sequence alignment are often sparse and uncertain. To some extent, these limitations in the data can be overcome by grouping the contacts by secondary structure elements and enumerating the possible packing arrangements of these elements in a combinatorial manner. Strong interactions appear frequently but inconsistent interactions are down-weighted and missing interactions up-weighted. The resulting improved consistency in the predicted interactions has allowed the method to be successfully applied to proteins up to 200 residues in length which is larger than any structure previously predicted using sequence data alone.

SUBMITTER: Taylor WR 

PROVIDER: S-EPMC3324774 | biostudies-literature | 2012 Feb

REPOSITORIES: biostudies-literature

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Protein topology from predicted residue contacts.

Taylor William R WR   Jones David T DT   Sadowski Michael I MI  

Protein science : a publication of the Protein Society 20111221 2


Residue contacts predicted from correlated positions in a multiple sequence alignment are often sparse and uncertain. To some extent, these limitations in the data can be overcome by grouping the contacts by secondary structure elements and enumerating the possible packing arrangements of these elements in a combinatorial manner. Strong interactions appear frequently but inconsistent interactions are down-weighted and missing interactions up-weighted. The resulting improved consistency in the pr  ...[more]

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