Expression and purification of human respiratory syncytial virus recombinant fusion protein

dc.contributorUniversidade Estadual Paulista (Unesp)
dc.contributorUniversidade de São Paulo (USP)
dc.contributorPontifícia Universidade Católica do Rio Grande do Sul (PUCRS)
dc.date.accessioned2014-05-20T14:00:30Z
dc.date.available2014-05-20T14:00:30Z
dc.date.created2014-05-20T14:00:30Z
dc.date.issued2008-12-01
dc.identifierProtein Expression and Purification. San Diego: Academic Press Inc. Elsevier B.V., v. 62, n. 2, p. 146-152, 2008.
dc.identifier1046-5928
dc.identifierhttp://hdl.handle.net/11449/21402
dc.identifier10.1016/j.pep.2008.08.005
dc.identifierWOS:000260598900002
dc.identifier7991082362671212
dc.identifier4101562077663619
dc.identifier0000-0001-5693-6148
dc.description.abstractThe Human Respiratory Syncytial Virus (HRSV) fusion protein (F) was expressed in Escherichia call BL21A using the pET28a vector at 37 degrees C. The protein was purified from the soluble fraction using affinity resin. The structural quality of the recombinant fusion protein and the estimation of its secondary structure were obtained by circular dichroism. Structural models of the fusion protein presented 46% of the helices in agreement with the spectra by circular dichroism analysis. There are only few studies that succeeded in expressing the HRSV fusion protein in bacteria. This is a report on human fusion protein expression in E. call and structure analysis, representing a step forward in the development of fusion protein F inhibitors and the production of antibodies. (c) 2008 Elsevier B.V. All rights reserved.
dc.languageeng
dc.publisherAcademic Press Inc. Elsevier B.V.
dc.relationProtein Expression and Purification
dc.relation1.338
dc.relation0,648
dc.rightsAcesso restrito
dc.sourceWeb of Science
dc.subjectFusion protein
dc.subjectPurification
dc.subjectDichroism analysis
dc.subjectMolecular modeling
dc.subjectExpression
dc.titleExpression and purification of human respiratory syncytial virus recombinant fusion protein
dc.typeArtículos de revistas


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