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dc.contributor.authorWinger, Moritzen_US
dc.contributor.authorvan⿿Gunsteren, Wilfred⿿F.en_US
dc.date.accessioned2017-04-24T13:40:28Z
dc.date.available2017-04-24T13:40:28Z
dc.date.issued2008en_US
dc.date.modified2011-05-03T04:46:42Z
dc.identifier.issn0018019Xen_US
dc.identifier.doi10.1002/hlca.200890175en_AU
dc.identifier.urihttp://hdl.handle.net/10072/38523
dc.description.abstractIn earlier work, two highly homologous (87% sequence identity) ankyrin repeat (AR) proteins, E3_5 and E3_19, were studied using molecular-dynamics (MD) simulation. Their stabilities were compared, and it was found that the C-terminal capping unit is unstable in the protein E3_19, in agreement with CD experiments. The different stabilities of these two very similar proteins could be explained by the different charge distributions among the AR units of the two proteins. Here, another AR protein, N3C, with yet another charge distribution has been simulated using MD, and its stability was analyzed. In agreement with the experimental data, the structure of N3C was found to be less stable than that of E3_5, but, in contrast to E3_19, secondary structure was only slightly lost, while structurally N3C is closer to E3_19 than to E3_5. The results suggest that a homogeneous charge distribution over the repeat units does enhance the stability of design AR proteins in aqueous solution, which, however, may be modulated by the bulkiness of amino-acid side chains involved in the mutations.en_US
dc.description.peerreviewedYesen_US
dc.description.publicationstatusYesen_AU
dc.languageEnglishen_US
dc.language.isoen_AU
dc.publisherVerlag Helvetica Chimica Actaen_US
dc.publisher.placeSwitzerlanden_US
dc.relation.ispartofstudentpublicationNen_AU
dc.relation.ispartofpagefrom1605en_US
dc.relation.ispartofpageto1613en_US
dc.relation.ispartofissue9en_US
dc.relation.ispartofjournalHelvetica Chimica Actaen_US
dc.relation.ispartofvolume91en_US
dc.rights.retentionYen_AU
dc.subject.fieldofresearchBiological Sciences not elsewhere classifieden_US
dc.subject.fieldofresearchcode069999en_US
dc.titleUse of molecular-dynamics simulation for optimizing protein stability: consensus-designed ankyrin repeaten_US
dc.typeJournal articleen_US
dc.type.descriptionC1 - Peer Reviewed (HERDC)en_US
dc.type.codeC - Journal Articlesen_US
gro.date.issued2008
gro.hasfulltextNo Full Text


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