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Updated: Mar 22, 2026

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web
Published on: July 16, 2017
Monitoring structural changes in intrinsically disordered proteins using QCM-D: application to the bacterial cell
Pablo Mateos-Gil1, Achilleas Tsortos2, Marisela Vélez1
1Instituto de Catálisis y Petroleoquímica (ICP-CSIC), c/MarieCurie 2, Cantoblanco, 28049 Madrid, Spain.
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.
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