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

Pablo Mateos-Gil; Achilleas Tsortos; Marisela Vélez; Electra Gizeli

doi:10.1039/c6cc02127a

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

Chem Commun (Camb). 2016 May 5;52(39):6541-4. doi: 10.1039/c6cc02127a.

Authors

Pablo Mateos-Gil¹, Achilleas Tsortos², Marisela Vélez¹, Electra Gizeli³

Affiliations

¹ Instituto de Catálisis y Petroleoquímica (ICP-CSIC), c/MarieCurie 2, Cantoblanco, 28049 Madrid, Spain.
² Institute of Molecular Biology & Biotechnology, FO.R.T.H, Vassilika Vouton, 70013, Heraklion, Greece.
³ Institute of Molecular Biology & Biotechnology, FO.R.T.H, Vassilika Vouton, 70013, Heraklion, Greece and Department of Biology, University of Crete, Vassilika Vouton, 71110, Heraklion, Greece. gizeli@imbb.forth.gr atsortos@imbb.forth.gr.

PMID: 27109863
DOI: 10.1039/c6cc02127a

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.

MeSH terms

Carrier Proteins / chemistry*
Cell Cycle Proteins / chemistry*
Escherichia coli Proteins / chemistry*
Intrinsically Disordered Proteins / chemistry*
Lipid Bilayers / chemistry
Protein Structure, Tertiary
Quartz Crystal Microbalance Techniques
Viscosity

Substances

Carrier Proteins
Cell Cycle Proteins
Escherichia coli Proteins
Intrinsically Disordered Proteins
Lipid Bilayers
ZipA protein, E coli