Detection of conformationally changed MBP using intramolecular FRET

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dc.contributor.authorK S Park-
dc.contributor.authorR H Lee-
dc.contributor.authorYong Beom Shin-
dc.contributor.authorSo Yeon Yi-
dc.contributor.authorY W Kang-
dc.contributor.authorD E Sok-
dc.contributor.authorJ W Chung-
dc.contributor.authorBong Hyun Chung-
dc.contributor.authorMoonil Kim-
dc.date.accessioned2017-04-19T09:14:33Z-
dc.date.available2017-04-19T09:14:33Z-
dc.date.issued2009-
dc.identifier.issn0006-291X-
dc.identifier.uri10.1016/j.bbrc.2009.08.049ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/9104-
dc.description.abstractThe principal objective of this study was to explore protein conformational changes using fluorescence resonance energy transfer (FRET) technology. Maltose binding protein (MBP) was adopted as a target model, due to its well-characterized structure and ligand specificity. To the best of our knowledge, this is the first report to provide information regarding the biological distance between the two lobes of MBP upon maltose binding. For the FRET pair, ECFP and EYFP were used as the donor and the acceptor, and were linked genetically to the C-terminal and N-terminal regions of MBP (ECFP:MBP:EYFP), respectively. After the FRET reaction, maltose-treated MBP was shown to exhibit a considerable energy transfer (FRET efficiency (E) = ∼0.11, Distance (D) = ∼6.93 nm) at the ensemble level, which was regarded as reflective of the increase in donor quenching and the upshift in acceptor emission intensity, thereby suggesting that the donor and the acceptor had been brought close together as the result of structural alterations in MBP. However, upon glucose treatment, no FRET phenomenon was detected, thereby implying the specificity of interaction between MBP and maltose. The in vitro FRET results were also confirmed via the acceptor photobleaching method. Therefore, our data showed that maltose-stimulated conformational changes of MBP could be measured by FRET, thereby providing biological information, including the FRET efficiency and the intramolecular distance.-
dc.publisherElsevier-
dc.titleDetection of conformationally changed MBP using intramolecular FRET-
dc.title.alternativeDetection of conformationally changed MBP using intramolecular FRET-
dc.typeArticle-
dc.citation.titleBiochemical and Biophysical Research Communications-
dc.citation.number3-
dc.citation.endPage564-
dc.citation.startPage560-
dc.citation.volume388-
dc.contributor.affiliatedAuthorYong Beom Shin-
dc.contributor.affiliatedAuthorSo Yeon Yi-
dc.contributor.affiliatedAuthorBong Hyun Chung-
dc.contributor.affiliatedAuthorMoonil Kim-
dc.contributor.alternativeName박경숙-
dc.contributor.alternativeName이란희-
dc.contributor.alternativeName신용범-
dc.contributor.alternativeName이소연-
dc.contributor.alternativeName강용원-
dc.contributor.alternativeName석대은-
dc.contributor.alternativeName정진웅-
dc.contributor.alternativeName정봉현-
dc.contributor.alternativeName김문일-
dc.identifier.bibliographicCitationBiochemical and Biophysical Research Communications, vol. 388, no. 3, pp. 560-564-
dc.identifier.doi10.1016/j.bbrc.2009.08.049-
dc.subject.keywordConformational change-
dc.subject.keywordFluorescence resonance energy transfer, FRET-
dc.subject.keywordMaltose binding protein, MBP-
dc.subject.localconformational change-
dc.subject.localConformational change-
dc.subject.localFluorescence resonance energy transfer, FRET-
dc.subject.localfluorescence resonance energy transfer-
dc.subject.localFRET-
dc.subject.localFluorescence resonance energy transfer-
dc.subject.localFluorescence resonance energy transfer (FRET)-
dc.subject.localMaltose Binding Protein-
dc.subject.localmaltose binding protein-
dc.subject.localmaltose binding protein (MBP)-
dc.subject.localMaltose-binding protein-
dc.subject.localMaltose binding protein, MBP-
dc.subject.localMaltose binding protein-
dc.description.journalClassY-
Appears in Collections:
Division of Research on National Challenges > Bionanotechnology Research Center > 1. Journal Articles
Critical Diseases Diagnostics Convergence Research Center > 1. Journal Articles
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