AI Article Synopsis
- This study utilizes QCM-D (Quartz Crystal Microbalance with Dissipation) to investigate how the protein ZipA changes shape in response to different salt concentrations.
- The technique effectively monitors the extension and contraction of ZipA's unstructured domain, revealing its molecular dynamics.
- The research shows a correlation between these conformational changes and variations in the protein's hydrodynamic radius, specifically changes of 1.8 nm or smaller.
Article 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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| http://dx.doi.org/10.1039/c6cc02127a | DOI Listing |
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