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      Monitoring molecular assembly of biofilms using quartz crystal microbalance with dissipation

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      Author(s)
      Yuca, E.
      Şeker, Urartu Özgür Şafak
      Editor
      Arluison, Véronique
      Wien, Frank
      Marcoleta, Andrés
      Date
      2022
      Source Title
      Bacterial amyloids: Methods and protocols
      Print ISSN
      1064-3745
      Publisher
      Springer
      Volume
      2538
      Pages
      25 - 33
      Language
      English
      Type
      Book Chapter
      Item Usage Stats
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      Book Title
      Bacterial amyloids: Methods and protocols
      Series
      Methods in Molecular Biology;
      Abstract
      The structure and the functionality of biofilm proteins, the main components of the extracellular matrix, can be tuned by protein engineering. The use of binding kinetics data has been demonstrated in the characterization of recombinantly produced biofilm proteins to control their behavior on certain surfaces or under certain conditions. Quartz crystal microbalance with dissipation monitoring (QCM-D) allows measuring the change in resonance frequency and the energy loss and distribution upon the interaction of molecules with the surface. The characterization of the molecular assembly of curli biofilm proteins on different surfaces using QCM-D is presented here as a detailed protocol. The experimental procedure detailed in this chapter can be applied and modified for other biofilm proteins or subunits to determine their surface adsorption and kinetic binding characteristics.
      Keywords
      Adsorption
      Amyloid
      Binding
      Biofilm
      Dissipation
      Kinetics
      Protein
      QCM-D
      Quartz sensor
      Surface
      Permalink
      http://hdl.handle.net/11693/111320
      Published Version (Please cite this version)
      https://www.doi.org/10.1007/978-1-0716-2529-3_3
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      • Institute of Materials Science and Nanotechnology (UNAM) 2258
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