Are you looking to reveal and validate the molecular mechanisms of DNA-binding proteins?

Getting direct, indisputable proof is possible now

You only need to look at your molecules in real time, one by one.

Capture molecular interactions

Enabling breakthrough discoveries

The C-Trap® is a dynamic single-molecule microscope that allows to visualize the dynamics of individual proteins. Its unique Nobel Prize winning technology allows – within the same experiment – to:

  • Obtain direct evidence of how the molecular mechanisms and dynamic processes of proteins on DNA work.
  • Observe the stepwise assembly of the biological complex.
  • Modulate the molecular system to test the model under different conditions.

This dynamic single-molecule technology is rapidly evolving as a mainstream approach in research for the study of DNA-binding proteins, molecular motor activity, protein folding, and protein droplets. Our systems are currently in use by core facilities molecular and structural biologists, biochemists, and biophysicists across the globe, including Stanford, JHU, Tsinghua University, and NIH. If you would like to get some inspiration from this technology, check out the following recent papers:

By using the C-Trap, >70% of papers are published in high impact factor journals.


Curious to understand how this can be applied to your research?

Download our webinar

Title: Dynamic Single-Molecule Approach to Directly Visualize the Molecular Mechanisms of DNA-Binding Proteins

Abstract: Studying DNA-binding proteins and validating the molecular mechanism of DNA processes often requires direct functional evidence. Here, we present the C-Trap: a new microscope that allows researchers to directly visualize the dynamics and assembly of the biological complex under different conditions – all at the single-molecule level, providing direct proof of the biological mechanism. We will showcase these functionalities with an example that directly visualizes the dynamical behavior of a helicase, how it activates at the replication fork, and how the replisome is assembled.

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