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Affinity Measurements Using Quartz Crystal Microbalance (QCM)

  • Thomas JohanssonEmail author
Protocol
Part of the Springer Protocols Handbooks book series (SPH)

To determine the affinity, the KD,-value, between interaction molecules a number of techniques using labels are available, such as chromatography, isothermal titration calorimetry, radioimmuno- assay and the widely used enzyme-linked immunosorbent assay (ELISA). However, need and developments have enabled studies of molecules interacting in real time using biosensors, without labeling or chemical modifications. In addition to KD, biosensors provide kinetic information about the interaction revealing the kinetic rate constants, kon and koff. Biosensors have been used to study a vast variety of molecular events, such as characterization of antibody–antigen, nucleic acid, and protein interactions. The Quartz Crystal Microbalance (QCM) technology is label-free and a direct way to determine affinity and kinetic rate constants. Here, we present describe the basic experimental design of typical kinetic strategies as well as data processing and interpretation with the aim of calculating affinity and rate constants of molecular interactions.

Keywords

Quartz Crystal Microbalance Isothermal Titration Calorimetry Sensor Surface Affinity Measurement Buffer Injection 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

References

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Copyright information

© Springer-Verlag Berlin Heidelberg 2010

Authors and Affiliations

  1. 1.Attana ABStockholmSweden

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