000054190 001__ 54190
000054190 005__ 20190625112052.0
000054190 0247_ $$2pmid$$apmid:17005536
000054190 0247_ $$2DOI$$a10.1093/bioinformatics/btl489
000054190 0247_ $$2WOS$$aWOS:000242715200007
000054190 0247_ $$2altmetric$$aaltmetric:3216061
000054190 037__ $$aPreJuSER-54190
000054190 041__ $$aeng
000054190 082__ $$a004
000054190 084__ $$2WoS$$aBiochemical Research Methods
000054190 084__ $$2WoS$$aBiotechnology & Applied Microbiology
000054190 084__ $$2WoS$$aComputer Science, Interdisciplinary Applications
000054190 084__ $$2WoS$$aMathematical & Computational Biology
000054190 084__ $$2WoS$$aStatistics & Probability
000054190 1001_ $$0P:(DE-Juel1)132307$$aZimmermann, O.$$b0$$uFZJ
000054190 245__ $$aSupport Vector Machines for Prediction of Dihedral Angle Regions
000054190 260__ $$aOxford$$bOxford University Press$$c2006
000054190 300__ $$a3009
000054190 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
000054190 3367_ $$2DataCite$$aOutput Types/Journal article
000054190 3367_ $$00$$2EndNote$$aJournal Article
000054190 3367_ $$2BibTeX$$aARTICLE
000054190 3367_ $$2ORCID$$aJOURNAL_ARTICLE
000054190 3367_ $$2DRIVER$$aarticle
000054190 440_0 $$013881$$aBioinformatics$$v22$$x1367-4803
000054190 500__ $$aRecord converted from VDB: 12.11.2012
000054190 520__ $$aMost secondary structure prediction programs target only alpha helix and beta sheet structures and summarize all other structures in the random coil pseudo class. However, such an assignment often ignores existing local ordering in so-called random coil regions. Signatures for such ordering are distinct dihedral angle pattern. For this reason, we propose as an alternative approach to predict directly dihedral regions for each residue as this leads to a higher amount of structural information.We propose a multi-step support vector machine (SVM) procedure, dihedral prediction (DHPRED), to predict the dihedral angle state of residues from sequence. Trained on 20,000 residues our approach leads to dihedral region predictions, that in regions without alpha helices or beta sheets is higher than those from secondary structure prediction programs.DHPRED has been implemented as a web service, which academic researchers can access from our webpage http://www.fz-juelich.de/nic/cbb
000054190 536__ $$0G:(DE-Juel1)FUEK411$$2G:(DE-HGF)$$aScientific Computing$$cP41$$x0
000054190 588__ $$aDataset connected to Web of Science, Pubmed
000054190 650_2 $$2MeSH$$aAlgorithms
000054190 650_2 $$2MeSH$$aAmino Acid Sequence
000054190 650_2 $$2MeSH$$aArtificial Intelligence
000054190 650_2 $$2MeSH$$aComputer Simulation
000054190 650_2 $$2MeSH$$aModels, Chemical
000054190 650_2 $$2MeSH$$aModels, Molecular
000054190 650_2 $$2MeSH$$aMolecular Sequence Data
000054190 650_2 $$2MeSH$$aPattern Recognition, Automated: methods
000054190 650_2 $$2MeSH$$aProtein Structure, Secondary
000054190 650_2 $$2MeSH$$aProteins: chemistry
000054190 650_2 $$2MeSH$$aProteins: ultrastructure
000054190 650_2 $$2MeSH$$aSequence Alignment: methods
000054190 650_2 $$2MeSH$$aSequence Analysis, Protein: methods
000054190 650_7 $$00$$2NLM Chemicals$$aProteins
000054190 650_7 $$2WoSType$$aJ
000054190 7001_ $$0P:(DE-Juel1)VDB46160$$aHansmann, U. H. E.$$b1$$uFZJ
000054190 773__ $$0PERI:(DE-600)1468345-3$$a10.1093/bioinformatics/btl489$$gVol. 22, p. 3009$$p3009$$q22<3009$$tBioinformatics$$v22$$x1367-4803$$y2006
000054190 8567_ $$uhttp://dx.doi.org/10.1093/bioinformatics/btl489
000054190 909CO $$ooai:juser.fz-juelich.de:54190$$pVDB
000054190 915__ $$0StatID:(DE-HGF)0010$$aJCR/ISI refereed
000054190 9141_ $$y2006
000054190 9131_ $$0G:(DE-Juel1)FUEK411$$bSchlüsseltechnologien$$kP41$$lSupercomputing$$vScientific Computing$$x0
000054190 9201_ $$0I:(DE-Juel1)NIC-20090406$$gNIC$$kNIC$$lJohn von Neumann - Institut für Computing$$x0
000054190 970__ $$aVDB:(DE-Juel1)84957
000054190 980__ $$aVDB
000054190 980__ $$aConvertedRecord
000054190 980__ $$ajournal
000054190 980__ $$aI:(DE-Juel1)NIC-20090406
000054190 980__ $$aUNRESTRICTED