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Enhanced protein domain discovery using taxonomy.

ABSTRACT: BACKGROUND: It is well known that different species have different protein domain repertoires, and indeed that some protein domains are kingdom specific. This information has not yet been incorporated into statistical methods for finding domains in sequences of amino acids. RESULTS: We show that by incorporating our understanding of the taxonomic distribution of specific protein domains, we can enhance domain recognition in protein sequences. We identify 4447 new instances of Pfam domains in the SP-TREMBL database using this technique, equivalent to the coverage increase given by the last 8.3% of Pfam families and to a 0.7% increase in the number of domain predictions. We use PSI-BLAST to cross-validate our new predictions. We also benchmark our approach using a SCOP test set of proteins of known structure, and demonstrate improvements relative to standard Hidden Markov model techniques. CONCLUSIONS: Explicitly including knowledge about the taxonomic distribution of protein domains can enhance protein domain recognition. Our method can also incorporate other context-specific domain distributions - such as domain co-occurrence and protein localisation.

SUBMITTER: Coin L

PROVIDER: S-EPMC434490 | biostudies-literature | 2004 May

REPOSITORIES: biostudies-literature

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Enhanced protein domain discovery using taxonomy.

Coin Lachlan L Bateman Alex A Durbin Richard R

BMC bioinformatics 20040511

<h4>Background</h4>It is well known that different species have different protein domain repertoires, and indeed that some protein domains are kingdom specific. This information has not yet been incorporated into statistical methods for finding domains in sequences of amino acids.<h4>Results</h4>We show that by incorporating our understanding of the taxonomic distribution of specific protein domains, we can enhance domain recognition in protein sequences. We identify 4447 new instances of Pfam d ...[more]

PMID: 15137915

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Project description:The assessment of examination questions is crucial in educational institutes since examination is one of the most common methods to evaluate students' achievement in specific course. Therefore, there is a crucial need to construct a balanced and high-quality exam, which satisfies different cognitive levels. Thus, many lecturers rely on Bloom's taxonomy cognitive domain, which is a popular framework developed for the purpose of assessing students' intellectual abilities and skills. Several works have been proposed to automatically handle the classification of questions in accordance with Bloom's taxonomy. Most of these works classify questions according to specific domain. As a result, there is a lack of technique of classifying questions that belong to the multi-domain areas. The aim of this paper is to present a classification model to classify exam questions based on Bloom's taxonomy that belong to several areas. This study proposes a method for classifying questions automatically, by extracting two features, TFPOS-IDF and word2vec. The purpose of the first feature was to calculate the term frequency-inverse document frequency based on part of speech, in order to assign a suitable weight for essential words in the question. The second feature, pre-trained word2vec, was used to boost the classification process. Then, the combination of these features was fed into three different classifiers; K-Nearest Neighbour, Logistic Regression, and Support Vector Machine, in order to classify the questions. The experiments used two datasets. The first dataset contained 141 questions, while the other dataset contained 600 questions. The classification result for the first dataset achieved an average of 71.1%, 82.3% and 83.7% weighted F1-measure respectively. The classification result for the second dataset achieved an average of 85.4%, 89.4% and 89.7% weighted F1-measure respectively. The finding from this study showed that the proposed method is significant in classifying questions from multiple domains based on Bloom's taxonomy.

Project description:BackgroundWe can describe protein-protein interactions (PPIs) as sets of distinct domain-domain interactions (DDIs) that mediate the physical interactions between proteins. Experimental data confirm that DDIs are more consistent than their corresponding PPIs, lending support to the notion that analyses of DDIs may improve our understanding of PPIs and lead to further insights into cellular function, disease, and evolution. However, currently available experimental DDI data cover only a small fraction of all existing PPIs and, in the absence of structural data, determining which particular DDI mediates any given PPI is a challenge.ResultsWe present two contributions to the field of domain interaction analysis. First, we introduce a novel computational strategy to merge domain annotation data from multiple databases. We show that when we merged yeast domain annotations from six annotation databases we increased the average number of domains per protein from 1.05 to 2.44, bringing it closer to the estimated average value of 3. Second, we introduce a novel computational method, parameter-dependent DDI selection (PADDS), which, given a set of PPIs, extracts a small set of domain pairs that can reconstruct the original set of protein interactions, while attempting to minimize false positives. Based on a set of PPIs from multiple organisms, our method extracted 27% more experimentally detected DDIs than existing computational approaches.ConclusionsWe have provided a method to merge domain annotation data from multiple sources, ensuring large and consistent domain annotation for any given organism. Moreover, we provided a method to extract a small set of DDIs from the underlying set of PPIs and we showed that, in contrast to existing approaches, our method was not biased towards DDIs with low or high occurrence counts. Finally, we used these two methods to highlight the influence of the underlying annotation density on the characteristics of extracted DDIs. Although increased annotations greatly expanded the possible DDIs, the lack of knowledge of the true biological false positive interactions still prevents an unambiguous assignment of domain interactions responsible for all protein network interactions.Executable files and examples are given at: http://www.bhsai.org/downloads/padds/

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Enhanced protein domain discovery using taxonomy.

Publications

Enhanced protein domain discovery using taxonomy.

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