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Full metadata record
DC Field | Value | Language |
---|---|---|
dc.citation.endPage | 987 | - |
dc.citation.number | 12 | - |
dc.citation.startPage | 981 | - |
dc.citation.title | NATURE CHEMICAL BIOLOGY | - |
dc.citation.volume | 11 | - |
dc.contributor.author | Min, Duyoung | - |
dc.contributor.author | Jefferson, Robet E. | - |
dc.contributor.author | Bowie, James U. | - |
dc.contributor.author | Yoon, Tae-Young | - |
dc.date.accessioned | 2023-12-22T00:38:34Z | - |
dc.date.available | 2023-12-22T00:38:34Z | - |
dc.date.created | 2019-10-04 | - |
dc.date.issued | 2015-10 | - |
dc.description.abstract | Membrane proteins are designed to fold and function in a lipid membrane, yet folding experiments within a native membrane environment are challenging to design. Here we show that single-molecule forced unfolding experiments can be adapted to study helical membrane protein folding under native-like bicelle conditions. Applying force using magnetic tweezers, we find that a transmembrane helix protein, Escherichia coli rhomboid protease GlpG, unfolds in a highly cooperative manner, largely unraveling as one physical unit in response to mechanical tension above 25 pN. Considerable hysteresis is observed, with refolding occurring only at forces below 5 pN. Characterizing the energy landscape reveals only modest thermodynamic stability (G = 6.5 k B T) but a large unfolding barrier (21.3 k B T) that can maintain the protein in a folded state for long periods of time (t 1/2 â 1/43.5 h). The observed energy landscape may have evolved to limit the existence of troublesome partially unfolded states and impart rigidity to the structure. © 2015 Nature America, Inc. | - |
dc.identifier.bibliographicCitation | NATURE CHEMICAL BIOLOGY, v.11, no.12, pp.981 - 987 | - |
dc.identifier.doi | 10.1038/nchembio.1939 | - |
dc.identifier.issn | 1552-4450 | - |
dc.identifier.scopusid | 2-s2.0-84947424922 | - |
dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/27806 | - |
dc.identifier.url | https://www.nature.com/articles/nchembio.1939 | - |
dc.identifier.wosid | 000365834000018 | - |
dc.language | 영어 | - |
dc.publisher | Nature Publishing Group | - |
dc.title | Mapping the energy landscape for second-stage folding of a single membrane protein | - |
dc.type | Article | - |
dc.description.isOpenAccess | FALSE | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.type.docType | Article | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.subject.keywordPlus | protein unfolding | - |
dc.subject.keywordPlus | tension | - |
dc.subject.keywordPlus | thermodynamics | - |
dc.subject.keywordPlus | chemical structure | - |
dc.subject.keywordPlus | chemistry | - |
dc.subject.keywordPlus | kinetics | - |
dc.subject.keywordPlus | metabolism | - |
dc.subject.keywordPlus | protein conformation | - |
dc.subject.keywordPlus | protein folding | - |
dc.subject.keywordPlus | Escherichia coli Proteins | - |
dc.subject.keywordPlus | Kinetics | - |
dc.subject.keywordPlus | Membrane Proteins | - |
dc.subject.keywordPlus | Models, Molecular | - |
dc.subject.keywordPlus | Protein Conformation | - |
dc.subject.keywordPlus | Protein Folding | - |
dc.subject.keywordPlus | Thermodynamics | - |
dc.subject.keywordPlus | bacterial protein | - |
dc.subject.keywordPlus | membrane protein | - |
dc.subject.keywordPlus | proteinase | - |
dc.subject.keywordPlus | rhomboid protease GlpG | - |
dc.subject.keywordPlus | unclassified drug | - |
dc.subject.keywordPlus | Escherichia coli protein | - |
dc.subject.keywordPlus | amino terminal sequence | - |
dc.subject.keywordPlus | Article | - |
dc.subject.keywordPlus | carboxy terminal sequence | - |
dc.subject.keywordPlus | energy | - |
dc.subject.keywordPlus | enzyme kinetics | - |
dc.subject.keywordPlus | Escherichia coli | - |
dc.subject.keywordPlus | hysteresis | - |
dc.subject.keywordPlus | nonhuman | - |
dc.subject.keywordPlus | priority journal | - |
dc.subject.keywordPlus | protein refolding | - |
dc.subject.keywordPlus | protein stability | - |
dc.subject.keywordPlus | protein structure | - |
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