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Article Dans Une Revue Data in Brief Année : 2016

Biophysical characterization data of the artificial protein Octarellin V.1 and binding test with its X-ray helpers

Résumé

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.

Dates et versions

hal-01355827 , version 1 (24-08-2016)

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Maximiliano Figueroa, Julie Vandenameele, Erik Goormaghtigh, Marie Valerio-Lepiniec, Philippe Minard, et al.. Biophysical characterization data of the artificial protein Octarellin V.1 and binding test with its X-ray helpers. Data in Brief, 2016, 8, ⟨10.1016/j.dib.2016.07.036⟩. ⟨hal-01355827⟩
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