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dc.contributor.authorSEO, JONGCHEOL-
dc.date.accessioned2022-02-25T06:00:07Z-
dc.date.available2022-02-25T06:00:07Z-
dc.date.created2022-02-24-
dc.date.issued2020-12-
dc.identifier.issn2233-4203-
dc.identifier.urihttps://oasis.postech.ac.kr/handle/2014.oak/109530-
dc.description.abstractDespite its great success in the field of proteomics, mass spectrometry has limited use for determining structural details of peptides, proteins, and their assemblies. Emerging ion mobility spectrometry-mass spectrometry has enabled us to explore the conformational space of protein ions in the gas phase, and further combinations with the gas-phase ion spectroscopy and the colli- sion-induced unfolding have extended its abilities to elucidating the secondary structure and local details of conformational transi- tions. This review will provide a brief introduction to the combined approaches of IMS-MS with gas-phase ion infrared spectroscopy or collision-induced unfolding and their most recent results that successfully revealed higher-order structural details.-
dc.languageEnglish-
dc.publisher사단법인 한국질량분석학회-
dc.relation.isPartOfMass Spectrometry Letters-
dc.titleAdvances in Ion Mobility Spectrometry-Mass Spectrometry (IMS-MS)-Based Techniques for Elucidating Higher-Order Protein Structures-
dc.typeArticle-
dc.identifier.doi10.5478/MSL.2020.11.4.65-
dc.type.rimsART-
dc.identifier.bibliographicCitationMass Spectrometry Letters, v.11, no.4, pp.65 - 70-
dc.identifier.kciidART002674401-
dc.citation.endPage70-
dc.citation.number4-
dc.citation.startPage65-
dc.citation.titleMass Spectrometry Letters-
dc.citation.volume11-
dc.contributor.affiliatedAuthorSEO, JONGCHEOL-
dc.identifier.scopusid2-s2.0-85101503732-
dc.description.journalClass1-
dc.description.journalClass1-
dc.description.isOpenAccessN-
dc.type.docTypeArticle-
dc.description.journalRegisteredClassscopus-
dc.description.journalRegisteredClasskci-

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