Monitoring structural changes in intrinsically disordered proteins using QCM-D: application to the bacterial cell division protein ZipA
2016
Mateos-GilCurrent address: Department of Biotechnology & Biophysics, University Wuerzburg, Germany. Pablo | Tsortos, Achilleas | Vélez, Marisela | Gizeli, Electra
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.
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