IRMPD and ECD fragmentation of intermolecular cross-linked peptides

dc.creatorSantos, LFA
dc.creatorEberlin, MN
dc.creatorGozzo, FC
dc.date2011
dc.dateMAR
dc.date2014-07-30T14:35:23Z
dc.date2015-11-26T16:26:42Z
dc.date2014-07-30T14:35:23Z
dc.date2015-11-26T16:26:42Z
dc.date.accessioned2018-03-28T23:07:33Z
dc.date.available2018-03-28T23:07:33Z
dc.identifierJournal Of Mass Spectrometry. Wiley-blackwell, v. 46, n. 3, n. 262, n. 268, 2011.
dc.identifier1076-5174
dc.identifierWOS:000288463900004
dc.identifier10.1002/jms.1891
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/60721
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/60721
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1268973
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.descriptionDespite the increasing number of studies using mass spectrometry for three dimensional analyses of proteins (MS3D), the identification of cross-linked peptides remains a bottleneck of the method. One of the main reasons for this is the lack of knowledge about the fragmentation of these species. Intermolecular cross-linked peptides are considered the most informative species present in MS3D experiment, since different peptides are connected by a cross-linker, the peptides chain can be either from a single protein, providing information about protein folding, or from two different proteins in a complex, providing information about binding partners, complex topology and interaction sites. These species tend to be large and highly charged in ESI, making comprehensive fragmentation by CID MS/MS problematic. On the other hand, these highly charged peptides are very suitable for dissociation using both infrared multiphoton dissociation (IRMPD) and electron capture dissociation (ECD). Herein, we report the fragmentation study of intermolecular cross-linked peptides using IRMPD and ECD. Using synthetic peptides and different commercial cross-linkers, a series of intermolecular cross-linked peptides were generate, and subsequently fragmented by IRMPD and ECD in a FT-ICR-MS instrument. Due to the high mass accuracy and resolution of the FT-ICR, the fragment ions could be attributed with high confidence. The peptides sequence coverage and fragmentation features obtained from IRMPD and ECD were compared for all charge states. Copyright (C) 2011 John Wiley & Sons, Ltd.
dc.description46
dc.description3
dc.description262
dc.description268
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.descriptionFAPESP [FAPESP 2004/14846-0, FINEP 01.07.0290.00]
dc.descriptionFAPESP [FAPESP 08/57805-2, CNPq 573672/2008-3]
dc.languageen
dc.publisherWiley-blackwell
dc.publisherMalden
dc.publisherEUA
dc.relationJournal Of Mass Spectrometry
dc.relationJ. Mass Spectrom.
dc.rightsfechado
dc.rightshttp://olabout.wiley.com/WileyCDA/Section/id-406071.html
dc.sourceWeb of Science
dc.subjectintermolecular cross-linked peptides
dc.subjectcross-linking
dc.subjectfragmentation
dc.subjectIRMPD
dc.subjectECD
dc.subjectElectron-capture Dissociation
dc.subjectProtein-protein Interactions
dc.subjectTandem Mass-spectrometry
dc.subjectConformational-changes
dc.subjectLinking
dc.subjectIdentification
dc.subjectComplexes
dc.subjectSites
dc.subjectQuaternary
dc.subjectAssignment
dc.titleIRMPD and ECD fragmentation of intermolecular cross-linked peptides
dc.typeArtículos de revistas


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