Abstract
In recent years there has been an explosive increase in the number of annotated protein sequences available through genome sequencing, as well as an accumulation of published protein structural data based on crystallographic and NMR methods. When taken together with the development of computational methods for the prediction of protein structural and functional properties through homology modeling, an opportunity exists for prediction of properties of cytoskeletal proteins in a suitable model organism, such as Tetrahymena thermophila and its ciliated protist relatives. In particular, the recently sequenced genome of T. thermophila, long a model for cytoskeletal studies, provides a good starting point for undertaking such homology modeling studies. Homology modeling can produce functional predictions, for example regarding potential molecular interactions, that are of great interest to the drug industry and Tetrahymena is an attractive model system in which to follow up computational predictions with experimental analyses. We provide here procedures that can be followed to gain entry into this promising avenue of analysis.
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Acknowledgements
Computational resources provided in part by the RI-INBRE Centralized Research Core Facility which is supported by an Institutional Development Award (IDeA) from the National Institute of General Medical Sciences of the National Institutes of Health under grant number 2 P20 GM103430.
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Pagano, G.J., Hufnagel, L.A., King, R.S. (2016). Homology Modeling Procedures for Cytoskeletal Proteins of Tetrahymena and Other Ciliated Protists. In: Gavin, R. (eds) Cytoskeleton Methods and Protocols. Methods in Molecular Biology, vol 1365. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-3124-8_24
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DOI: https://doi.org/10.1007/978-1-4939-3124-8_24
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