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Issue 39, 2016
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Monitoring structural changes in intrinsically disordered proteins using QCM-D: application to the bacterial cell division protein ZipA

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Abstract

The sensitivity of QCM-D to molecular hydrodynamic properties is applied in this work to study conformational changes of the intrinsically disordered protein ZipA. Acoustic measurements can clearly follow ZipA's unstructured domain expansion and contraction with salt content and be correlated with changes in the hydrodynamic radius of 1.8 nm or less.

Graphical abstract: Monitoring structural changes in intrinsically disordered proteins using QCM-D: application to the bacterial cell division protein ZipA

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Publication details

The article was received on 10 Mar 2016, accepted on 11 Apr 2016 and first published on 11 Apr 2016


Article type: Communication
DOI: 10.1039/C6CC02127A
Author version available: Download Author version (PDF)
Citation: Chem. Commun., 2016,52, 6541-6544
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    Monitoring structural changes in intrinsically disordered proteins using QCM-D: application to the bacterial cell division protein ZipA

    P. Mateos-Gil, A. Tsortos, M. Vélez and E. Gizeli, Chem. Commun., 2016, 52, 6541
    DOI: 10.1039/C6CC02127A

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