Kinetics – Affinity – Avidity
Conformational Changes


Join us for our Basic Binding Kinetics Tutorial!


In this 20 min tutorial, learn how easy it is to measure binding kinetics with our new heliX® biosensors. We´ll be analyzing both association and dissociation rates as well as Kd-values, using only 8 pmol/run of sample at a cost of just 1.30 EUR per datapoint.

Learn how heliX® enables you to characterize molecular interactions in a user friendly, cost effective, and reproducible way.

switchSENSE® Technology
Molecular Interaction Analysis
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  • Binding Kinetics
  • Binding Affinity
  • Protein Diameter
  • Conformational Change
  • Nuclease & Polymerase Activity
  • Bispecific Binders & Avidity
  • Melting & Thermodynamics
  • Multimers & Aggregation

Application Areas

Introducing heliX®


The dynamicBIOSENSORS team is excited to announce the launch of the heliX® line of biosensor instruments!

heliX® pushes the boundaries of what has been possible in biosensing to help you do more:

Analysis of binding kinetics and molecular conformations in one measurement.

Screening of conformational changes de novo by real-time conformation referencing.

Resolving the fastest kinetics with confidence using advanced microfluidics and 10 ms data collection, and taking advantage of improved signal stability for the characterization of high-affinity binders in long dissociation measurements.

Two-color single-photon counting fluorescence detection for femto-molar sensitivity and the in-depth analysis of bispecific binders.

Effortless sensor functionalization and advanced ligand density control with the new Adapter Chip.

heliX® is based on a modular technical design and features an automatic chip-loader in conjunction with a 384 well plate compatible autosampler, allowing you to scale-up throughput to thousands of samples per day.

In focus

Browse through the latest publications.

Paper in Analytical Biochemistry I 19 July 2020

Nucleotide binding kinetics and conformational change analysis of tissue transglutaminase with switchSENSE

In this publication, we introduce switchSENSE® as a versatile tool for TG2 characterization and provide novel insights into protein conformation as well as analyte binding kinetics. For the first time, we succeeded in measuring the kinetic rate constants and affinities (kon, koff, KD) for guanosine nucleotides (GMP, GDP, GTP, GTPγS). Further, the conformational changes induced by GDP, Ca2+ and the covalent inhibitor Z-DON were observed by changes in TG2’s hydrodynamic diameter. We confirmed the well-known compaction by guanosine nucleotides and extension by Ca2+, and provide evidence for TG2 conformations so far not described by structural analysis. Moreover, we analyze the influence of the peptidic Z-DON inhibitor and the R580A mutation on the conformational responsiveness of TG2 to its natural effectors. In summary, this work shows how the combination of structural and kinetic information obtained by switchSENSE® opens new perspectives for the characterization of conformationally active proteins and their interactions with ligands, e.g. potential drug candidates.


Paper in Scientific Reports I 09 June 2020

The trimer to monomer transition of Tumor Necrosis Factor-Alpha is a dynamic process that is significantly altered by therapeutic antibodies

In this paper, we demonstrate the power of switchSENSE® for size analysis and antibody binding kinetics. In certain inflammatory diseases, such as rheumatoid arthritis, TNF-α is upregulated and forms bioactive homotrimers that promote inflammation. This bioactivation that was previously reported to occur over hours is seen to occur in only minutes when measured in real-time using switchSENSE’s dynamic measurement mode. The kinetics of TNF-α targeting therapeutic antibodies, including HUMIRA, are also observed, including the long dissociation (measured over 30,000 sec!) of TNF-α from these tight binders. This novel approach also sheds some light on the strong differences between these antibodies that were previously thought to have the same mode of action.


Paper in PNAS I 31 March 2020

An autoinhibitory intramolecular interaction proof-reads RNA recognition by the essential splicing factor U2AF2

switchSENSE® resolves the binding kinetics of the splicing factor U2AF2 to a target RNA sequence. Hyun-Seo Kang of Michael Sattler’s workgroup at the Technical University of Munich used switchSENSE® to confirm the regulatory function on RNA binding of an inter-domain linker in U2AF2 by measuring the association- and dissociation kinetics of the wildtype protein and of a mutant in which the regulatory linker region had been rendered inactive.


→ click here for a list of all switchSENSE® publications.

Dr. Michael Schraeml, Head Protein and Enzyme Technologies

Products for High-Performance Analysis


switchSENSE® experiments are performed on reusable multi-electrode, multi-channels biochips.

DRX Instruments

Fully automated switchSENSE® instruments are 96-well plates compatible and manufactured in Germany.


Including coupling kits, starter packs, training & OQ kits, as well as buffers, solutions and other consumables.


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