dc.contributorUniversidade de São Paulo (USP)
dc.contributorUniversidade Federal de Mato Grosso do Sul (UFMS)
dc.contributorUniversidade Estadual Paulista (Unesp)
dc.contributorUniversidade Federal do Rio de Janeiro (UFRJ)
dc.contributorPontifícia Universidade Católica do Rio Grande do Sul (PUCRS)
dc.date.accessioned2014-05-20T13:24:36Z
dc.date.accessioned2022-10-05T13:14:18Z
dc.date.available2014-05-20T13:24:36Z
dc.date.available2022-10-05T13:14:18Z
dc.date.created2014-05-20T13:24:36Z
dc.date.issued2006-06-01
dc.identifierProtein Expression and Purification. San Diego: Academic Press Inc. Elsevier B.V., v. 47, n. 2, p. 614-620, 2006.
dc.identifier1046-5928
dc.identifierhttp://hdl.handle.net/11449/7685
dc.identifier10.1016/j.pep.2006.02.012
dc.identifierWOS:000238277000034
dc.identifier4101562077663619
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/3884499
dc.description.abstractThe human cyclin-dependent kinase 9 (CDK9) protein was expressed in E coli BL21 using the pET23a vector at 30 degrees C. Several milligrams of protein were purified from soluble fraction using ionic exchange and ATP-affinity chromatography. The structural quality of recombinant CDK9 and the estimation of its secondary structure were obtained by circular dichroism. Structural models of CDK9 presented 26% of helices in agreement with the spectra by circular dichroism analysis. This is the first report on human CDK9 expression in Escherichia coli and structure analysis and provides the first step for the development of CDK9 inhibitors. (c) 2006 Elsevier B.V. All rights reserved.
dc.languageeng
dc.publisherElsevier B.V.
dc.relationProtein Expression and Purification
dc.relation1.338
dc.relation0,648
dc.rightsAcesso restrito
dc.sourceWeb of Science
dc.subjectCDK9
dc.subjectCâncer
dc.subjectAIDS
dc.subjectStructure
dc.subjectdichroism analysis
dc.subjectmolecular modeling
dc.subjectexpression
dc.titleExpression, purification, and circular dichroism analysis of human CDK9
dc.typeArtigo


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