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Folding of Circularly Permuted and Split Outer Membrane Protein F via Electrostatic Interactions with Terminal Residues

DC Field Value Language
dc.contributor.authorLee, Jaewon-
dc.contributor.authorSong, Woon Ju-
dc.date.accessioned2024-05-16T01:51:03Z-
dc.date.available2024-05-16T01:51:03Z-
dc.date.created2021-07-21-
dc.date.created2021-07-21-
dc.date.issued2021-06-
dc.identifier.citationBiochemistry, Vol.60 No.23, pp.1787-1796-
dc.identifier.issn0006-2960-
dc.identifier.urihttps://hdl.handle.net/10371/202916-
dc.description.abstractMembrane proteins are essential targets in drug design, biosensing, and catalysis. In this study, we explored the folding of engineered outer membrane protein F (OmpF), an abundant and functional beta-barrel protein expressed in Gram-negative bacteria. We carried out circular permutation, splitting and self-complementation, and point mutation. The folding efficiency and kinetic analyses demonstrated that the N- and C-terminal residues of OmpF played critical roles in folding via electrostatic interactions with lipid headgroups. Our results indicate that native porins without charged terminal residues may be tightly down-regulated to retain the integrity of the outer membrane, and this modification may facilitate the insertion and folding of modified membrane proteins under in vitro and in vivo conditions for various applications.-
dc.language영어-
dc.publisherAmerican Chemical Society-
dc.titleFolding of Circularly Permuted and Split Outer Membrane Protein F via Electrostatic Interactions with Terminal Residues-
dc.typeArticle-
dc.identifier.doi10.1021/acs.biochem.1c00195-
dc.citation.journaltitleBiochemistry-
dc.identifier.wosid000663933900001-
dc.identifier.scopusid2-s2.0-85108304019-
dc.citation.endpage1796-
dc.citation.number23-
dc.citation.startpage1787-
dc.citation.volume60-
dc.description.isOpenAccessN-
dc.contributor.affiliatedAuthorSong, Woon Ju-
dc.type.docTypeArticle-
dc.description.journalClass1-
dc.subject.keywordPlusOMPF PORIN-
dc.subject.keywordPlusINSERTION-
dc.subject.keywordPlusRECONSTITUTION-
dc.subject.keywordPlusDISPLAY-
dc.subject.keywordPlusOLIGOMERIZATION-
dc.subject.keywordPlusSTABILITY-
dc.subject.keywordPlusEVOLUTION-
dc.subject.keywordPlusVARIANTS-
dc.subject.keywordPlusSURFACE-
dc.subject.keywordPlusLIPIDS-
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  • College of Natural Sciences
  • Department of Chemistry
Research Area Biochemistry, Inorganic, 무기화학, 생화학

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