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Using MemBlob to Analyze Transmembrane Regions Based on Cryo-EM Maps.
Csizmadia, Georgina; Farkas, Bianka; Katona, Eszter; Tusnády, Gábor E; Hegedus, Tamás.
Afiliación
  • Csizmadia G; Department of Biophysics and Radiation Biology, Semmelweis University, Budapest, Hungary.
  • Farkas B; MTA-SE Molecular Biophysics Research Group, Hungarian Academy of Sciences, Budapest, Hungary.
  • Katona E; Department of Biophysics and Radiation Biology, Semmelweis University, Budapest, Hungary.
  • Tusnády GE; MTA-SE Molecular Biophysics Research Group, Hungarian Academy of Sciences, Budapest, Hungary.
  • Hegedus T; Faculty of Information Technology and Bionics, Pázmány Péter Catholic University, Budapest, Hungary.
Methods Mol Biol ; 2112: 123-130, 2020.
Article en En | MEDLINE | ID: mdl-32006282
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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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Microscopía por Crioelectrón / Proteínas de la Membrana Idioma: En Revista: Methods Mol Biol Asunto de la revista: BIOLOGIA MOLECULAR Año: 2020 Tipo del documento: Article País de afiliación: Hungria

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Microscopía por Crioelectrón / Proteínas de la Membrana Idioma: En Revista: Methods Mol Biol Asunto de la revista: BIOLOGIA MOLECULAR Año: 2020 Tipo del documento: Article País de afiliación: Hungria
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