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Analysis of the thermostability determinants of hyperthermophilic esterase EstE1 based on its predicted three-dimensional structure

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dc.contributor.authorRhee, JK-
dc.contributor.authorKim, DY-
dc.contributor.authorAhn, DG-
dc.contributor.authorYun, JH-
dc.contributor.authorJang, SH-
dc.contributor.authorShin, HC-
dc.contributor.authorCho, HS-
dc.contributor.authorPan, JG-
dc.contributor.authorOh, JW-
dc.date.available2018-05-10T17:11:00Z-
dc.date.created2018-04-17-
dc.date.issued2006-04-
dc.identifier.issn0099-2240-
dc.identifier.urihttp://scholarworks.bwise.kr/ssu/handle/2018.sw.ssu/18646-
dc.description.abstractThe three-dimensional (3D) structure of the hyperthermophilic esterase EstE1 was constructed by homology modeling using Archaeoglobus fulgidus esterase as a reference, and the thermostability-structure relationship was analyzed. Our results verified the predicted 3D structure of EstE1 and identified the ion pair networks and hydrophobic interactions that are critical determinants for the thermostability of EstE1.-
dc.publisherAMER SOC MICROBIOLOGY-
dc.relation.isPartOfAPPLIED AND ENVIRONMENTAL MICROBIOLOGY-
dc.subjectHORMONE-SENSITIVE LIPASE-
dc.subjectTHERMAL-STABILITY-
dc.subjectCRYSTAL-STRUCTURE-
dc.subjectADAPTATION-
dc.subjectPROTEINS-
dc.subjectSEQUENCE-
dc.subjectENZYME-
dc.subjectFAMILY-
dc.titleAnalysis of the thermostability determinants of hyperthermophilic esterase EstE1 based on its predicted three-dimensional structure-
dc.typeArticle-
dc.identifier.doi10.1128/AEM.72.4.3021-3025.2006-
dc.type.rimsART-
dc.identifier.bibliographicCitationAPPLIED AND ENVIRONMENTAL MICROBIOLOGY, v.72, no.4, pp.3021 - 3025-
dc.description.journalClass1-
dc.identifier.wosid000236749400090-
dc.identifier.scopusid2-s2.0-33646088728-
dc.citation.endPage3025-
dc.citation.number4-
dc.citation.startPage3021-
dc.citation.titleAPPLIED AND ENVIRONMENTAL MICROBIOLOGY-
dc.citation.volume72-
dc.contributor.affiliatedAuthorShin, HC-
dc.type.docTypeArticle-
dc.description.oadoiVersionpublished-
dc.subject.keywordPlusHORMONE-SENSITIVE LIPASE-
dc.subject.keywordPlusTHERMAL-STABILITY-
dc.subject.keywordPlusCRYSTAL-STRUCTURE-
dc.subject.keywordPlusADAPTATION-
dc.subject.keywordPlusPROTEINS-
dc.subject.keywordPlusSEQUENCE-
dc.subject.keywordPlusENZYME-
dc.subject.keywordPlusFAMILY-
dc.description.journalRegisteredClassscopus-
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