Biblioteca Digital

**Autoria(s):** Leopoldino, A. M.; Canduri, F.; Cabral, H.; Junqueira, M.; Marqui, A, B. T. de; Apponi, L. H.; da Fonseca, I. O.; Domont, G. B.; Santos, D. S.; Valentini, S.; Bonilla-Rodriguez, G. O.; Fossey, Marcelo Andrés; Azevedo, W. F. de; Tajara, E. H.
Contribuinte(s)	Universidade Estadual Paulista (UNESP)
Data(s)	20/05/2014 20/05/2014 01/06/2006
Resumo	The 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.
Formato	614-620
Identificador	http://dx.doi.org/10.1016/j.pep.2006.02.012 Protein Expression and Purification. San Diego: Academic Press Inc. Elsevier B.V., v. 47, n. 2, p. 614-620, 2006. 1046-5928 http://hdl.handle.net/11449/7685 10.1016/j.pep.2006.02.012 WOS:000238277000034
Idioma(s)	eng
Publicador	Elsevier B.V.
Relação	Protein Expression and Purification
Direitos	closedAccess
Palavras-Chave	#CDK9 #Câncer #AIDS #Structure #dichroism analysis #molecular modeling #expression
Tipo	info:eu-repo/semantics/article

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