Biophysical characterization data of the artificial protein Octarellin V.1 and binding test with its X-ray helpers
Maximiliano Figueroa,
Julie Vandenameele,
Erik Goormaghtigh,
Marie Valerio-Lepiniec,
Philippe Minard,
André Matagne,
Cécile Van de Weerdt
Affiliations
Maximiliano Figueroa
GIGA-Research, Molecular Biomimetics and Protein Engineering, University of Liège, Liège, Belgium; Biochemistry and Molecular Biology Department, University of Concepcion, Concepción, Chile; Corresponding authors.
Julie Vandenameele
Laboratoire d’Enzymologie et Repliement des Protéines, Centre for Protein Engineering, University of Liège, Liège, Belgium
Erik Goormaghtigh
Laboratory for the Structure and Function of Biological Membranes, Center for Structural Biology and Bioinformatics, Université Libre de Bruxelles, Brussels, Belgium
Marie Valerio-Lepiniec
Institute for Integrative Biology of the Cell (I2BC), UMT 9198, CEA, CNRS, Université Paris-Sud, Orsay, France
Philippe Minard
Institute for Integrative Biology of the Cell (I2BC), UMT 9198, CEA, CNRS, Université Paris-Sud, Orsay, France
André Matagne
Laboratoire d’Enzymologie et Repliement des Protéines, Centre for Protein Engineering, University of Liège, Liège, Belgium
Cécile Van de Weerdt
GIGA-Research, Molecular Biomimetics and Protein Engineering, University of Liège, Liège, Belgium; Corresponding authors.
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. Keywords: Artificial proteins, Circular dichroism, Crystallization helpers, Infra red spectroscopy, Protein design, Isothermal Titration Calorimetry
