Abstract
Previous study shows that the same type of bond lengths and angles fit Gaussian distributions well with small standard deviations on high resolution protein structure data. The mean values of these Gaussian distributions have been widely used as ideal bond lengths and angles in bioinformatics. However, we are not aware of any research work done to evaluate how accurately we can model protein structures with dihedral angles and ideal bond lengths and angles.
In this paper, we first introduce the protein structure idealization problem. Then, we develop a fast O(nm / ε) dynamic programming algorithm to find an approximately optimal idealized protein backbone structure according to our scoring function. Consequently, we demonstrate that idealized backbone structures always exist with small changes and significantly better free energy. We also apply our algorithm to refine protein pseudo-structures determined in NMR experiments.
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Cui, X., Li, S.C., Bu, D., Alipanahi Ramandi, B., Li, M. (2012). How Accurately Can We Model Protein Structures with Dihedral Angles?. In: Raphael, B., Tang, J. (eds) Algorithms in Bioinformatics. WABI 2012. Lecture Notes in Computer Science(), vol 7534. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-33122-0_22
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DOI: https://doi.org/10.1007/978-3-642-33122-0_22
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