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dc.contributor.authorAlves, V. S.
dc.contributor.authorPimenta, D. C.
dc.contributor.authorSattlegger, E.
dc.contributor.authorCastilho, B. A.
dc.date.accessioned2016-01-24T12:34:15Z
dc.date.available2016-01-24T12:34:15Z
dc.date.issued2004-01-30
dc.identifierhttp://dx.doi.org/10.1016/j.bbrc.2003.12.086
dc.identifier.citationBiochemical and Biophysical Research Communications. San Diego: Academic Press Inc Elsevier Science, v. 314, n. 1, p. 229-234, 2004.
dc.identifier.issn0006-291X
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/27586
dc.description.abstractGir2 is an uncharacterized protein of Saccharomyces cerevisiae, containing a RWD/GI domain. in this work, we report the biophysical characterization of Gir2. His-tagged Gir2, expressed and purified from Escherichia coli, showed an abnormally slow migration on SDS-PAGE. the yeast expressed protein behaves similarly. Using mass spectrometry and peptide mass fingerprinting we demonstrated that the protein has the expected molecular mass (34 kDa). EDC modification of carboxylate groups reverted the anomalous migration on SDS-PAGE. Size exclusion chromatography showed that Gir2 has a Stokes radius larger than expected. Gir2 is thermostable and lacks extensive structure, as determined by CD analysis. Based on these findings, we suggest that Gir2 is a representative of the growing group of natively unfolded proteins. (C) 2003 Elsevier Inc. All rights reserved.en
dc.format.extent229-234
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofBiochemical and Biophysical Research Communications
dc.rightsAcesso restrito
dc.subjectGir2en
dc.subjecthighly acidicen
dc.subjectanomalous behavioren
dc.subjectnatively unfoldeden
dc.titleBiophysical characterization of Gir2, a highly acidic protein of Saccharomyces cerevisiae with anomalous electrophoretic behavioren
dc.typeArtigo
dc.rights.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.contributor.institutionCtr Toxincol Aplicada
dc.contributor.institutionNICHHD
dc.description.affiliationUniversidade Federal de São Paulo, Escola Paulista Med, Dept Microbiol Immunol & Parasitol, São Paulo, SP, Brazil
dc.description.affiliationCtr Toxincol Aplicada, CAT, CEPID, Inst Butantan, São Paulo, SP, Brazil
dc.description.affiliationNICHHD, NIH, Bethesda, MD 20892 USA
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Escola Paulista Med, Dept Microbiol Immunol & Parasitol, São Paulo, SP, Brazil
dc.identifier.doi10.1016/j.bbrc.2003.12.086
dc.description.sourceWeb of Science
dc.identifier.wosWOS:000188250200034


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