Introducing pure protein-DNA conjugates

proFIRE® is a unique system for protein-DNA conjugate preparation,
delivering consistent and superior conjugate quality for your experiments.

smart biophysical analysis

Electrically switchable nanolevers –
the switchSENSE® principle

switchSENSE® Technology
Molecular Interaction Analysis
Powered by
Electro-switchable Nanolevers
Unrivaled Information Content

read more >

  • Binding Kinetics
  • Binding Affinity
  • Protein Diameter
  • Conformational Change
  • Nuclease & Polymerase Activity
  • Bispecific Binders & Avidity
  • Melting & Thermodynamics
  • Multimers & Aggregation

Application Areas

Spot our Highlights & News

Pure protein-DNA conjugates

Introducing proFIRE® – a unique system for protein-DNA conjugate preparation.

Video Portrait

Go-Bio video portrait about Dynamic Biosensors and switchSENSE® technology.

Our New FAQ Section is Online!

We present you a comprehensive knowledge base for all your queries about switchSENSE®.

User Meeting 2018

We would like to thank all our customers and participants for a successful switchSENSE® User Meeting!

New Capture Kit

Introducing the ultra-stable
Strep-Tactin®XT Kit

New Chief Sales & Marketing Officer

Dr. Martin Greber has been appointed the new Chief Sales & Marketing Officer

New Labs & Office Space in USA

Opening of our application labs and office in San Diego, CA / USA

Launch of MP3 Chip

Launch of switchSENSE®chip
with three densities

In Focus

Paper in Nature 2018

ANKRD16 prevents neuron loss caused by an editing-defective tRNA synthetase

In the recent work published in Nature, researchers from The Scripps Research Institute report on the novel role that protein ANKRD16 plays in the complex process of protein aggregate-associated neurodegeneration. Vo and Terrey et al demonstrated that in the absence of ANKRD16, neuron loss is induced by the aggregation of proteins mistranslated by tRNA synthetases that carry a mutation in their editing domain. ANKRD16 is found to act as a translational co-factor, contributing to the prevention of mistranslation.

read more >

Using the switchSENSE® technology, the kinetics of binding of ANKRD16 to wild-type, mutated and truncated tRNA synthetase variants were measured. The measurements for the direct binding of ANKRD16 to the different tRNA synthetase variants shed light on the mechanism of ANKRD16 recognition of misactivated amino acid sequences, as well as the location of its binding to the tRNA synthetase, critical to describing ANKRD16’s protective role in neurodegeneration.

Editing domains of aminoacyl tRNA synthetases correct tRNA charging errors to maintain translational fidelity. A mutation in the editing domain of alanyl tRNA synthetase (AlaRS) in Aarssti mutant mice results in an increase in the production of serine-mischarged tRNAAla and the degeneration of cerebellar Purkinje cells. Here, using positional cloning, we identified Ankrd16, a gene that acts epistatically with the Aarsstimutation to attenuate neurodegeneration. ANKRD16, a vertebrate-specific protein that contains ankyrin repeats, binds directly to the catalytic domain of AlaRS. Serine that is misactivated by AlaRS is captured by the lysine side chains of ANKRD16, which prevents the charging of serine adenylates to tRNAAla and precludes serine misincorporation in nascent peptides. The deletion of Ankrd16 in the brains of Aarssti/sti mice causes widespread protein aggregation and neuron loss. These results identify an amino-acid-accepting co-regulator of tRNA synthetase editing as a new layer of the machinery that is essential to the prevention of severe pathologies that arise from defects in editing.

Paper in JBC 2018

A low-complexity region in the YTH domain protein Mmi1 enhances RNA binding

In a recent publication in the Journal of Biological Chemistry, researchers from the MRC Laboratory of Molecular Biology (LMB), show how a low complexity region enhances RNA binding by the YTH domain protein Mmi1, using the switchSENSE® technology.

Taken together, the work reveals how a low-complexity region proximal to a conserved folded domain can adopt an ordered structure to aid nucleic acid binding.

read more >

Mmi1 is an essential RNA-binding protein in the fission yeast Schizosaccharomyces pombe that eliminates meiotic transcripts during normal vegetative growth. Mmi1 contains a YTH domain that binds specific RNA sequences, targeting mRNAs for degradation. The YTH domain of Mmi1 uses a noncanonical RNA-binding surface that includes contacts outside the conserved fold. Here, we report that an N-terminal extension that is proximal to the YTH domain enhances RNA binding. Using X-ray crystallography, NMR and biophysical methods, we show that this low-complexity region becomes more ordered upon RNA binding.

This enhances the affinity of the interaction of the Mmi1 YTH domain with specific RNAs by reducing the dissociation rate of the Mmi1–RNA complex. We propose that the low-complexity region influences RNA binding indirectly by reducing dynamic motions of the RNA binding groove and stabilizing a conformation of the YTH domain that binds to RNA with high affinity. Taken together, our work reveals how a low-complexity region proximal to a conserved folded domain can adopt an ordered structure to aid nucleic acid binding.

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.

User Statements

Dr. Michael Schraeml, Head Protein and Enzyme Technologies


What are you interested in? *

Consumables & Reagents
Technical Support
Quotes & Orders

Instruments & Applications
Technical & Software Support
Assay Development

New to switchSENSE®
General Info & Evaluation

Dynamic Biosensors Data Privacy Policy

Contact Specialist