J Chem Inf Model - Crowdsourcing yields a new standard for kinks in protein helices.

Tópicos

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Resumo

Kinks are functionally important structural features found in the a-helices of proteins. Structurally, they are points at which a helix abruptly changes direction. Current kink definition and identification methods often disagree with one another. Here we describe a crowdsourcing approach to obtain a reliable gold standard set of kinks. Using an online interface, we collected more than 10,000 classifications of 300 helices into straight, curved, or kinked categories. We found that participants were better at discriminating between straight and not-straight helices than between kinked and curved helices. Surprisingly, more obvious kinks were not necessarily identified as more localized within the helix. We present a set of 252 helices where more than 50% of the participants agree on a classification. This set can be used as a reliable gold standard to develop, train, and compare computational methods. An interactive visualization of the results is available online at http://opig.stats.ox.ac.uk/webapps/ahah/php/experiment_results.php .

Resumo Limpo

kink function import structur featur found ahelic protein structur point helix abrupt chang direct current kink definit identif method often disagre one anoth describ crowdsourc approach obtain reliabl gold standard set kink use onlin interfac collect classif helic straight curv kink categori found particip better discrimin straight notstraight helic kink curv helic surpris obvious kink necessarili identifi local within helix present set helic particip agre classif set can use reliabl gold standard develop train compar comput method interact visual result avail onlin httpopigstatsoxacukwebappsahahphpexperimentresultsphp

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