Abstract
Transmembrane proteins include membrane channels, pores, and receptors and, as such, comprise an important part of the proteome, yet our knowledge about them is much less complete than about soluble, globular proteins. An important aspect of transmembrane protein structure is their exact position within the lipid bilayer, a feature hard to investigate experimentally at the atomic level. Here we describe MemBlob, a novel approach utilizing difference electron density maps obtained by cryo-EM studies of transmembrane proteins. The idea behind is that the nonprotein part of such maps carries information on the exact localization of the membrane mimetics used in the experiment and can be used to extract the positional information of the protein within the membrane. MemBlob uses a structural model of the protein and an experimental electron density map to provide an estimation of the surface residues interacting with the membrane.
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Acknowledgments
This work has been supported by grants from the National Research, Development and Innovation Office NKFIH K111678, NKFIH K119287, NKFIH K125607, and NKFIH K127961, the Cystic Fibrosis Foundation (CFF HEGEDU18I0), and the Semmelweis Science and Innovation Fund.
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Csizmadia, G., Farkas, B., Katona, E., Tusnády, G.E., Hegedűs, T. (2020). Using MemBlob to Analyze Transmembrane Regions Based on Cryo-EM Maps. In: Gáspári, Z. (eds) Structural Bioinformatics. Methods in Molecular Biology, vol 2112. Humana, New York, NY. https://doi.org/10.1007/978-1-0716-0270-6_9
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DOI: https://doi.org/10.1007/978-1-0716-0270-6_9
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