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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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Supplementary files

Article information


Submitted
10 Mar 2016
Accepted
11 Apr 2016
First published
11 Apr 2016

Chem. Commun., 2016,52, 6541-6544
Article type
Communication
Author version available

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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