Issue 39, 2016
From the journal:

Chemical Communications

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

Pablo Mateos-Gil,‡a   Achilleas Tsortos,*b   Marisela Véleza  and  Electra Gizeli*bc  

* Corresponding authors

a Instituto de Catálisis y Petroleoquímica (ICP-CSIC), c/MarieCurie 2, Cantoblanco, 28049 Madrid, Spain

b Institute of Molecular Biology & Biotechnology, FO.R.T.H, Vassilika Vouton, Heraklion, Greece

c Department of Biology, University of Crete, Vassilika Vouton, Heraklion, Greece
E-mail: gizeli@imbb.forth.gr, atsortos@imbb.forth.gr

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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Article information

DOI
https://doi.org/10.1039/C6CC02127A
Article type
Communication
Submitted
10 Mar 2016
Accepted
11 Apr 2016
First published
11 Apr 2016

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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