Maltoporin LamB Unfolds β Hairpins along Mechanical Stress-Dependent Unfolding Pathways

Thoma, Johannes and Ritzmann, Noah and Wolf, Dominik and Mulvihill, Estefania and Hiller, Sebastian and Müller, Daniel J.. (2017) Maltoporin LamB Unfolds β Hairpins along Mechanical Stress-Dependent Unfolding Pathways. Structure, 25 (7). pp. 1139-1144.e2.

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Upon mechanical pulling at either terminal end, β barrel outer membrane proteins stepwise unfold β strands or β hairpins until entirely extracted from the membrane. This unique unfolding pathway has been described for β barrels comprising 8, 14, or 22 β strands. Here we mechanically unfold the 18-stranded β barrel outer membrane protein LamB from Escherichia coli. We find that its mechanical unfolding pathway is shaped by the stepwise unfolding of β hairpins. However, we also observe that β hairpins can unfold groupwise. Thereby, β hairpins unfolding at higher pulling forces show a higher probability to unfold collectively, whereas β hairpins unfolding at lower forces tend to unfold individually. This result suggests that the collective unfolding of β hairpins resembles a far-from-equilibrium process, whereas the unfolding of individual β hairpins describes a closer-to-equilibrium process. Our findings support a direct link between outer membrane protein structure and the unfolding pathway and contribute to a better understanding of their unfolding in response to mechanical stress.
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
Publisher:Elsevier (Cell Press)
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:30 May 2018 07:24
Deposited On:30 May 2018 07:24

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