Expression and purification of human respiratory syncytial virus recombinant fusion protein
| Contribuinte(s) |
Universidade Estadual Paulista (UNESP) |
|---|---|
| Data(s) |
20/05/2014
20/05/2014
01/12/2008
|
| Resumo |
Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP) Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq) Processo FAPESP: 02/08461-2 The 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. |
| Formato |
146-152 |
| Identificador |
http://dx.doi.org/10.1016/j.pep.2008.08.005 Protein Expression and Purification. San Diego: Academic Press Inc. Elsevier B.V., v. 62, n. 2, p. 146-152, 2008. 1046-5928 http://hdl.handle.net/11449/21402 10.1016/j.pep.2008.08.005 WOS:000260598900002 |
| Idioma(s) |
eng |
| Publicador |
Academic Press Inc. Elsevier B.V. |
| Relação |
Protein Expression and Purification |
| Direitos |
closedAccess |
| Palavras-Chave | #Fusion protein #Purification #Dichroism analysis #Molecular modeling #Expression |
| Tipo |
info:eu-repo/semantics/article |
