DC Field | Value | Language |
---|---|---|
dc.contributor.author | jong park | ko |
dc.contributor.author | sabine dietmann | ko |
dc.contributor.author | andreas heger | ko |
dc.contributor.author | liisa holm | ko |
dc.date.accessioned | 2013-02-27T22:21:52Z | - |
dc.date.available | 2013-02-27T22:21:52Z | - |
dc.date.created | 2012-02-06 | - |
dc.date.created | 2012-02-06 | - |
dc.date.issued | 2000 | - |
dc.identifier.citation | BIOINFORMATICS, v.16, no.11, pp.978 - 987 | - |
dc.identifier.issn | 1367-4803 | - |
dc.identifier.uri | http://hdl.handle.net/10203/71179 | - |
dc.description.abstract | Motivation: How critical is the sequence order information in predicting protein secondary structure segments? We tried to get a rough insight on it from a theoretical approach using both a prediction algorithm and structural fragments from Protein Databank (PDB). Results: Using reverse protein sequences and PDB structural fragments, we theoretically estimated the significance of the order for protein secondary structure and prediction. On average: (1) 79% of protein sequence segments resulted in the same prediction in both normal and reverse directions, which indicated a relatively high conservation of secondary structure propensity in the reverse direction; (2) the reversed sequence prediction alone performed less accurately than the normal forward sequence prediction, but comparably high (2% difference); (3) the commonly predicted regions showed a slightly higher prediction accuracy (4%) than the normal sequences prediction; and (4) structural fragments which have counterparts in reverse direction in the same protein showed a comparable degree of secondary structure conservation (73% identity with reversed structures on average for pentamers). | - |
dc.language | English | - |
dc.publisher | Oxford Univ Press | - |
dc.subject | FOLD RECOGNITION | - |
dc.subject | GLOBULAR-PROTEINS | - |
dc.subject | ALIGNMENT | - |
dc.subject | IDENTIFICATION | - |
dc.subject | DATABASE | - |
dc.subject | ACCURACY | - |
dc.subject | IMPROVEMENTS | - |
dc.subject | PERFORMANCE | - |
dc.subject | PARAMETERS | - |
dc.subject | HOMOLOGY | - |
dc.title | Estimating the significance of sequence order in protein secondary structure prediction. | - |
dc.type | Article | - |
dc.identifier.wosid | 000166343700004 | - |
dc.identifier.scopusid | 2-s2.0-0034521885 | - |
dc.type.rims | ART | - |
dc.citation.volume | 16 | - |
dc.citation.issue | 11 | - |
dc.citation.beginningpage | 978 | - |
dc.citation.endingpage | 987 | - |
dc.citation.publicationname | BIOINFORMATICS | - |
dc.identifier.doi | 10.1093/bioinformatics/16.11.978 | - |
dc.contributor.localauthor | jong park | - |
dc.contributor.nonIdAuthor | sabine dietmann | - |
dc.contributor.nonIdAuthor | andreas heger | - |
dc.contributor.nonIdAuthor | liisa holm | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordPlus | FOLD RECOGNITION | - |
dc.subject.keywordPlus | GLOBULAR-PROTEINS | - |
dc.subject.keywordPlus | ALIGNMENT | - |
dc.subject.keywordPlus | IDENTIFICATION | - |
dc.subject.keywordPlus | DATABASE | - |
dc.subject.keywordPlus | ACCURACY | - |
dc.subject.keywordPlus | IMPROVEMENTS | - |
dc.subject.keywordPlus | PERFORMANCE | - |
dc.subject.keywordPlus | PARAMETERS | - |
dc.subject.keywordPlus | HOMOLOGY | - |
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