Biophysics Department, Faculty of Science, Cairo University, Giza, 12613, Egypt
In this work, the native state of zebrafish arbin protein was modeled from protein
sequence and was refined using solution X-ray scattering. The sequence of zebrafish arbin was
converted to 3D structure using Iterative Threading Assembly Refinement Program (I_TASSER). The
experimental X-ray scattering profile was fitted to theoretical X-ray profile of zebrafish arbin model
by CRYSOL Program, and the chi error was 8.517. Zebrafish arbin model was superimposed to its
average shape by SUPREF Program and the distance between them was 4.715. The Phi and Psi
angles of amino acids of zebrafish arbin model were altered using Phi and Psi Change Tool of SwisspdbViewer.
The chi and distance of the zebrafish arbin model were decreased to 3.421 and 2.255,
respectively. 3D structure of many proteins can be solved by this method without the need of protein
crystallization and complicated crystallographic technique.
Key words: Zebrafish arbin, protein structure, X-ray scattering.
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