The electrostatic core of the outer membrane protein X from E. coli

Rath, Parthasarathi and Sharpe, Timothy and Hiller, Sebastian. (2020) The electrostatic core of the outer membrane protein X from E. coli. Biochimica et Biophysica Acta (BBA) - Biomembranes, 1862 (1). p. 183031.

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Electrostatic side chain contacts can contribute substantial interaction energy terms to the stability of proteins. The impact of electrostatic interactions on the structure and architecture of outer membrane proteins is however not well studied compared to soluble proteins. Here, we report the results of a systematic study of all charged side chains of the E. coli outer membrane protein X (OmpX). The data identify three distinct salt-bridge clusters in the core of OmpX that contribute significantly to protein stability in dodecylphosphocholine detergent micelles. The three clusters form an "electrostatic core" of the membrane protein OmpX, corresponding in its architectural role to the hydrophobic core of soluble proteins. This article is part of a Special Issue entitled: Molecular biophysics of membranes and membrane proteins.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Structural Biology & Biophysics > Structural Biology (Hiller)
UniBasel Contributors:Hiller Odermatt, Sebastian and Sharpe, Timothy and Rath, Parthasarathi
Item Type:Article, refereed
Article Subtype:Research Article
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:10 Feb 2020 16:20
Deposited On:10 Feb 2020 16:20

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