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Biophysical characterization data of the artificial protein Octarellin V.1 and binding test with its X-ray helpers.
Figueroa, Maximiliano; Vandenameele, Julie; Goormaghtigh, Erik; Valerio-Lepiniec, Marie; Minard, Philippe; Matagne, André; Van de Weerdt, Cécile.
Afiliação
  • Figueroa M; GIGA-Research, Molecular Biomimetics and Protein Engineering, University of Liège, Liège, Belgium; Biochemistry and Molecular Biology Department, University of Concepcion, Concepción, Chile.
  • Vandenameele J; Laboratoire d'Enzymologie et Repliement des Protéines, Centre for Protein Engineering, University of Liège, Liège, Belgium.
  • Goormaghtigh E; Laboratory for the Structure and Function of Biological Membranes, Center for Structural Biology and Bioinformatics, Université Libre de Bruxelles, Brussels, Belgium.
  • Valerio-Lepiniec M; Institute for Integrative Biology of the Cell (I2BC), UMT 9198, CEA, CNRS, Université Paris-Sud, Orsay, France.
  • Minard P; Institute for Integrative Biology of the Cell (I2BC), UMT 9198, CEA, CNRS, Université Paris-Sud, Orsay, France.
  • Matagne A; Laboratoire d'Enzymologie et Repliement des Protéines, Centre for Protein Engineering, University of Liège, Liège, Belgium.
  • Van de Weerdt C; GIGA-Research, Molecular Biomimetics and Protein Engineering, University of Liège, Liège, Belgium.
Data Brief ; 8: 1221-6, 2016 Sep.
Article em En | MEDLINE | ID: mdl-27547801
The artificial protein Octarellin V.1 (http://dx.doi.org/10.1016/j.jsb.2016.05.004[1]) was obtained through a direct evolution process over the de novo designed Octarellin V (http://dx.doi.org/10.1016/S0022-2836(02)01206-8[2]). The protein has been characterized by circular dichroism and fluorescence techniques, in order to obtain data related to its thermo and chemical stability. Moreover, the data for the secondary structure content studied by circular dichroism and infra red techniques is reported for the Octarellin V and V.1. Two crystallization helpers, nanobodies (http://dx.doi.org/10.1038/nprot.2014.039[3]) and αRep (http://dx.doi.org/10.1016/j.jmb.2010.09.048[4]), have been used to create stable complexes. Here we present the data obtained of the binding characterization of the Octarellin V.1 with the crystallization helpers by isothermal titration calorimetry.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Idioma: En Revista: Data Brief Ano de publicação: 2016 Tipo de documento: Article País de afiliação: Chile País de publicação: Holanda
Texto completo
Adicionar na Minha BVS
Imprimir
XML
PubMed Links
Buscar no Google

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Idioma: En Revista: Data Brief Ano de publicação: 2016 Tipo de documento: Article País de afiliação: Chile País de publicação: Holanda