Artificial proteins; Circular dichroism; Crystallization helpers; Infra red spectroscopy; Isothermal Titration Calorimetry; Protein design
Abstract :
[en] 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 alphaRep (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.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Figueroa Yévenes, Maximiliano ; Université de Liège > Département des sciences de la vie > GIGA-R : Biologie et génétique moléculaire
Vandenameele, Julie ; Université de Liège > Département des sciences de la vie > Centre d'ingénierie des protéines
Goormaghtigh, Erik
Valerio-Lepiniec, Marie
Minard, Philippe
Matagne, André ; Université de Liège > Département des sciences de la vie > Enzymologie et repliement des protéines
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