Monitoring structural changes in intrinsically disordered proteins using QCM-D: application to the bacterial cell division protein ZipA.
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.
Instituto de Catálisis y Petroleoquímica (ICP-CSIC), c/MarieCurie 2, Cantoblanco, 28049 Madrid, Spain.
Pablo
P
Mateos-Gil
Institute of Molecular Biology & Biotechnology, FO.R.T.H, Vassilika Vouton, 70013, Heraklion, Greece.
Achilleas
A
Tsortos
Instituto de Catálisis y Petroleoquímica (ICP-CSIC), c/MarieCurie 2, Cantoblanco, 28049 Madrid, Spain.
Marisela
M
Vélez
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.
Electra
E
Gizeli
D002352:Carrier Proteins / Q000737:chemistry*; D018797:Cell Cycle Proteins / Q000737:chemistry*; D029968:Escherichia coli Proteins / Q000737:chemistry*; D064267:Intrinsically Disordered Proteins / Q000737:chemistry*; D008051:Lipid Bilayers / Q000737:chemistry; D017434:Protein Structure, Tertiary; D058525:Quartz Crystal Microbalance Techniques; D014783:Viscosity
D002352:Carrier Proteins; D018797:Cell Cycle Proteins; D029968:Escherichia coli Proteins; D064267:Intrinsically Disordered Proteins; D008051:Lipid Bilayers; C103795:ZipA protein, E coli