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

详细信息    查看全文

• 作者：Maximiliano Figueroa^a ; ^b ; ^{maxifigueroa@udec.cl" class="auth_mail" title="E-mail the corresponding author} ; Julie Vandenameele^c ; Erik Goormaghtigh^d ; Marie Valerio-Lepiniec^e ; Philippe Minard^e ; André ; Matagne^c ; Cé ; cile Van de Weerdt^a ; ^{c.vandeweerdt@ulg.ac.be" class="auth_mail" title="E-mail the corresponding author}
• 关键词：Artificial proteins ; Circular dichroism ; Crystallization helpers ; Infra red spectroscopy ; Protein design ; Isothermal Titration Calorimetry
• 刊名：Data in Brief
• 出版年：2016
• 出版时间：September 2016
• 年：2016
• 卷：8
• 期：Complete
• 页码：1221-1226
• 全文大小：986 K

文摘

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.