Monitoring Backbone Hydrogen-Bond Formation in β-Barrel Membrane Protein Folding

Raschle, Thomas and Rios Flores, Perla and Opitz, Christian and Müller, Daniel J. and Hiller, Sebastian. (2016) Monitoring Backbone Hydrogen-Bond Formation in β-Barrel Membrane Protein Folding. Angewandte Chemie. International edition in English, 55 (20). pp. 5952-5955.

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Official URL: http://edoc.unibas.ch/43204/

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β-barrel membrane proteins are key components of the outer membrane of bacteria, mitochondria and chloroplasts. Their three-dimensional structure is defined by a network of backbone hydrogen bonds between adjacent β-strands. Here, we employ hydrogen-deuterium (H/D) exchange in combination with NMR spectroscopy and mass spectrometry to monitor backbone hydrogen bond formation during folding of the outer membrane protein X (OmpX) from E. coli in detergent micelles. Residue-specific kinetics of interstrand hydrogen-bond formation were found to be uniform in the entire β-barrel and synchronized to formation of the tertiary structure. OmpX folding thus propagates via a long-lived conformational ensemble state in which all backbone amide protons exchange with the solvent and engage in hydrogen bonds only transiently. Stable formation of the entire OmpX hydrogen bond network occurs downhill of the rate-limiting transition state and thus appears cooperative on the overall folding time scale.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Structural Biology & Biophysics > Structural Biology (Hiller)
UniBasel Contributors:Hiller Odermatt, Sebastian
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:20 Dec 2017 15:05
Deposited On:06 Dec 2016 08:11

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