DC Field | Value | Language |
---|---|---|
dc.contributor.author | Skorupka, K | - |
dc.contributor.author | Han, SK | - |
dc.contributor.author | Nam, HJ | - |
dc.contributor.author | Kim, S | - |
dc.contributor.author | Faham, S | - |
dc.date.accessioned | 2015-06-23T07:00:29Z | - |
dc.date.available | 2015-06-23T07:00:29Z | - |
dc.date.created | 2014-02-26 | - |
dc.date.issued | 2013-12 | - |
dc.identifier.issn | 0907-4449 | - |
dc.identifier.other | 2015-OAK-0000028947 | en_US |
dc.identifier.uri | https://oasis.postech.ac.kr/handle/2014.oak/9287 | - |
dc.description.abstract | Domain fusion is a useful tool in protein design. Here, the structure of a fusion of the heterodimeric flagella-assembly proteins FliS and FliC is reported. Although the ability of the fusion protein to maintain the structure of the heterodimer may be apparent, threading-based structural predictions do not properly fuse the heterodimer. Additional examples of naturally occurring heterodimers that are homologous to full-length proteins were identified. These examples highlight that the designed protein was engineered by the same tools as used in the natural evolution of proteins and that heterodimeric structures contain a wealth of information, currently unused, that can improve structural predictions. | - |
dc.description.statementofresponsibility | open | en_US |
dc.language | English | - |
dc.publisher | International Union of Crystallography | - |
dc.relation.isPartOf | Acta Crystallographica Section D | - |
dc.rights | BY_NC_ND | en_US |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/2.0/kr | en_US |
dc.title | Protein design by fusion: implications for protein structure prediction and evolution | - |
dc.type | Article | - |
dc.contributor.college | 생명과학과 | en_US |
dc.identifier.doi | 10.1107/S0907444913022701 | - |
dc.author.google | Skorupka, K | en_US |
dc.author.google | Han, SK | en_US |
dc.author.google | Nam, HJ | en_US |
dc.author.google | Kim, S | en_US |
dc.author.google | Faham, S | en_US |
dc.relation.volume | 69 | en_US |
dc.relation.issue | 12 | en_US |
dc.relation.startpage | 2451 | en_US |
dc.relation.lastpage | 2460 | en_US |
dc.contributor.id | 10136479 | en_US |
dc.relation.journal | Acta Crystallographica Section D | en_US |
dc.relation.index | SCI급, SCOPUS 등재논문 | en_US |
dc.relation.sci | SCI | en_US |
dc.collections.name | Journal Papers | en_US |
dc.type.rims | ART | - |
dc.identifier.bibliographicCitation | Acta Crystallographica Section D, v.69, no.12, pp.2451 - 2460 | - |
dc.identifier.wosid | 000328370400018 | - |
dc.date.tcdate | 2019-01-01 | - |
dc.citation.endPage | 2460 | - |
dc.citation.number | 12 | - |
dc.citation.startPage | 2451 | - |
dc.citation.title | Acta Crystallographica Section D | - |
dc.citation.volume | 69 | - |
dc.contributor.affiliatedAuthor | Kim, S | - |
dc.identifier.scopusid | 2-s2.0-84889775982 | - |
dc.description.journalClass | 1 | - |
dc.description.journalClass | 1 | - |
dc.description.wostc | 2 | - |
dc.description.scptc | 1 | * |
dc.date.scptcdate | 2018-10-274 | * |
dc.type.docType | Article | - |
dc.subject.keywordPlus | RANDOM CIRCULAR PERMUTATION | - |
dc.subject.keywordPlus | STRUCTURE ALIGNMENT | - |
dc.subject.keywordPlus | CRYSTAL-STRUCTURES | - |
dc.subject.keywordPlus | DATABASE | - |
dc.subject.keywordPlus | DOMAINS | - |
dc.subject.keywordPlus | FOLD | - |
dc.subject.keywordPlus | GENERATION | - |
dc.subject.keywordPlus | PEPTIDE | - |
dc.subject.keywordPlus | CLASSIFICATION | - |
dc.subject.keywordPlus | RECOGNITION | - |
dc.relation.journalWebOfScienceCategory | Biochemical Research Methods | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Biophysics | - |
dc.relation.journalWebOfScienceCategory | Crystallography | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalResearchArea | Biophysics | - |
dc.relation.journalResearchArea | Crystallography | - |
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