Analysis of secondary structure in proteins by chemical cross-linking coupled to MS

dc.creatorFioramonte, M
dc.creatordos Santos, AM
dc.creatorMcIlwain, S
dc.creatorNoble, WS
dc.creatorFranchini, KG
dc.creatorGozzo, FC
dc.date2012
dc.dateAUG
dc.date2014-07-30T13:49:00Z
dc.date2015-11-26T16:06:22Z
dc.date2014-07-30T13:49:00Z
dc.date2015-11-26T16:06:22Z
dc.date.accessioned2018-03-28T22:55:11Z
dc.date.available2018-03-28T22:55:11Z
dc.identifierProteomics. Wiley-blackwell, v. 12, n. 17, n. 2746, n. 2752, 2012.
dc.identifier1615-9853
dc.identifierWOS:000308098700016
dc.identifier10.1002/pmic.201200040
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/54601
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/54601
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1265897
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.descriptionChemical cross-linking is an attractive technique for the study of the structure of protein complexes due to its low sample consumption and short analysis time. Furthermore, distance constraints obtained from the identification of cross-linked peptides by MS can be used to construct and validate protein models. If a sufficient number of distance constraints are obtained, then determining the secondary structure of a protein can allow inference of the protein's fold. In this work, we show how the distance constraints obtained from cross-linking experiments can identify secondary structures within the protein sequence. Molecular modeling of alpha helices and beta sheets reveals that each secondary structure presents different cross-linking possibilities due to the topological distances between reactive residues. Cross-linking experiments performed with amine reactive cross-linkers with model alpha helix containing proteins corroborated the molecular modeling predictions. The cross-linking patterns established here can be extended to other cross-linkers with known lengths for the determination of secondary structures in proteins.
dc.description12
dc.description17
dc.descriptionSI
dc.description2746
dc.description2752
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.descriptionInstituto Nacional de Ciencia e Tecnologia em Bioanalitica (INCTBio)
dc.descriptionGenoprot Program for Intracelular Peptides
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.languageen
dc.publisherWiley-blackwell
dc.publisherHoboken
dc.publisherEUA
dc.relationProteomics
dc.relationProteomics
dc.rightsfechado
dc.rightshttp://olabout.wiley.com/WileyCDA/Section/id-406071.html
dc.sourceWeb of Science
dc.subjectAlpha helix
dc.subjectBeta sheet
dc.subjectCross-linking
dc.subjectMS
dc.subjectProtein secondary structure
dc.subjectTechnology
dc.subjectMass-spectrometry
dc.subjectStructure Prediction
dc.subjectIdentification
dc.subjectConstraints
dc.subjectComplex
dc.subjectLinker
dc.titleAnalysis of secondary structure in proteins by chemical cross-linking coupled to MS
dc.typeArtículos de revistas


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