Please use this identifier to cite or link to this item: http://doi.org/10.25358/openscience-279
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dc.contributor.authorBrüne, Daniel-
dc.contributor.authorAndrade, Miguel-
dc.contributor.authorMier, Pablo-
dc.date.accessioned2019-01-23T10:18:50Z-
dc.date.available2019-01-23T11:18:50Z-
dc.date.issued2018-
dc.identifier.urihttps://openscience.ub.uni-mainz.de/handle/20.500.12030/281-
dc.description.abstractObjective Amino acid composition is a sequence feature that has been extensively used to characterize proteomes of many species and protein families. Yet the analysis of amino acid composition of protein domains and the linkers connecting them has received less attention. Here, we perform both a comprehensive full-proteome amino acid composition analysis and a similar analysis focusing on domains and linkers, to uncover domain- or linker-specific differential amino acid usage patterns. Results The amino acid composition in the 38 proteomes studied showcase the greater variability found in archaea and bacteria species compared to eukaryotes. When focusing on domains and linkers, we describe the preferential use of polar residues in linkers and hydrophobic residues in domains. To let any user perform this analysis on a given domain (or set of them), we developed a dedicated R script called RACCOON, which can be easily used and can provide interesting insights into the compositional differences between a domain and its surrounding linkers.en_GB
dc.description.sponsorshipDFG, Open Access-Publizieren Universität Mainz / Universitätsmedizin-
dc.language.isoeng-
dc.rightsCC BYde_DE
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/-
dc.subject.ddc570 Biowissenschaftende_DE
dc.subject.ddc570 Life sciencesen_GB
dc.titleProteome-wide comparison between the amino acid composition of domains and linkersen_GB
dc.typeZeitschriftenaufsatzde_DE
dc.identifier.doihttp://doi.org/10.25358/openscience-279-
jgu.type.dinitypearticle-
jgu.type.versionPublished versionen_GB
jgu.type.resourceText-
jgu.organisation.departmentFB 10 Biologie-
jgu.organisation.number7970-
jgu.organisation.nameJohannes Gutenberg-Universität Mainz-
jgu.rights.accessrightsopenAccess-
jgu.journal.titleBMC Research Notes-
jgu.journal.volume11-
jgu.pages.alternativeArt. 117-
jgu.publisher.year2018-
jgu.publisher.nameBioMed Central-
jgu.publisher.placeLondon-
jgu.publisher.urihttp://dx.doi.org/10.1186/s13104-018-3221-0-
jgu.publisher.issn1756-0500-
jgu.notes.publicAndrade, Miguel veröffentlicht unter: Andrade-Navarro, Miguel A.de_DE
jgu.organisation.placeMainz-
jgu.subject.ddccode570-
opus.date.accessioned2019-01-23T10:18:50Z-
opus.date.modified2019-01-23T10:38:11Z-
opus.date.available2019-01-23T11:18:50-
opus.subject.dfgcode00-000-
opus.organisation.stringFB 10: Biologie: Institut für Organismische und Molekulare Evolutionsbiologiede_DE
opus.identifier.opusid58799-
opus.institute.number1011-
opus.metadataonlyfalse-
opus.type.contenttypeKeinede_DE
opus.type.contenttypeNoneen_GB
opus.affiliatedAndrade, Miguel-
opus.affiliatedMier, Pablo-
jgu.publisher.doi10.1186/s13104-018-3221-0
jgu.organisation.rorhttps://ror.org/023b0x485
Appears in collections:JGU-Publikationen

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