Only structural and functional 

data is not enough

Observe your protein on DNA in real-time to directly connect its molecular mechanisms to its clinical impact.

Find out how you can gain these unique insights

Mechanisms are by their nature dynamic. This is combined with the challenge that not all mechanisms act the same way all of the time. How can you get the insight you need to fully understand your protein DNA binding mechanism? Read our application note 

Important highlights:

– Direct evidence of the DNA/protein binding site

– New insights into clinical impact uncovered

– How unambiguous, direct evidence was obtained

Understanding how DNA-binding proteins interact with DNA is key

For example, by looking at the interactions of POLQ with DNA, a recent study suggests that the inhibition of its DNA-repair capabilities could play a synergetic role with the inhibition of another DNA repair protein, PARP. Indeed, targeting both proteins in novel cancer therapies could result in the efficient killing of cancer cells.

Adapted from Belan et al. Molecular Cell (2022)

Watch this 60s summary video!

Current methods often struggles to reveal the dynamic molecular mechanism of individual proteins on DNA 

The protein’s molecular function can be inferred through methods that examine its detailed static structure or average behavior. However, these methods are often unable to reveal some of the crucial mechanistic details that are only accessible when studied:

Looking dynamically

DNA-protein interactions are inherently dynamic. Not only are the beginning and end states important, but all the intermediate states too. These can only be captured by a dynamic movie looking at every step of the process

In real-time

Watching a dynamic movie of DNA-protein interactions in real-time gives the ability to have a direct influence over the movie, as it unfolds. This enables unique conditions and functions to be investigated

At the single-molecule level

When looking at a large number of proteins, the average protein function can hide sub-population or individual behaviors. Behaviors that are functionally key and that are only visible when looking at a single protein

With great experimental control

Having control over one specific piece of DNA, which proteins it is interacting with and in which condition it is really unlocks unique ways to probe and understand protein function

What if a method exists that fulfills all these requirements?

A dynamic single-molecule method for direct, indisputable proof of the detailed molecular mechanisms

Directly visualize the location and dynamics of individual biomolecules

Control the stepwise assembly of the biological complex

Modulate molecular conformations while observing changes as they happen

The C-Trap® is the world’s first
dynamic single-molecule instrument

Designed to capture detailed DNA-binding protein interactions in real-time,
effortlessly, leading you in no time to highly impactful discoveries.

We are trusted worldwide by key opinion leaders that are already using the C-Trap to conduct highly impactful science

Senior vice-president at Artios Pharma Ltd and senior group leader at the Francis Crick Institute in London

An expert in DNA repair and the treatment of cancer resulting from DNA damage.

“I think applications like [single-molecule approaches] will become more mainstream in terms of understanding DNA transaction-based reactions and how small molecules interfere with that.”

Group leader at Vrije Universiteit Amsterdam

An expert in the physics of life processes.

“The combination of fluorescence with optical tweezers is one of the biggest steps [forward], it allows studying the most complex interactions between protein and DNA.”

Distinguished Professor of Microbiology and Molecular Genetics at the University of California at Davis.

An expert in biochemistry and the molecular biology of DNA repair and homologous recombination.

“The optical tweezers enable easy manipulation of single-DNA molecules [and] single-protein complexes on those DNA molecules.”

Top C-Trap publications you can’t miss

Greenhough L. A. et al, Structure and mechanism of action of the RAD51BCD-XRCC2 tumour suppressor complex, Nature, 2023 (Simon Boulton & Steve West, The Francis Crick Institute, London, UK)

Anand, R. et al. HELQ is a dual-function DSB repair enzyme modulated by RPA and RAD51. Nature, 2021. (Simon Boulton, The Francis Crick Institute, London, UK)

Wasserman, M. et al. Replication Fork Activation Is Enabled by a Single-Stranded DNA Gate in CMG Helicase. Cell 2019. (Shixin Liu & Michael O’Donnel, Rockefeller University, New York, US)

Ling Wang et. al., Head-on and co-directional RNA polymerase collisions orchestrate bidirectional transcription termination. Molecular Cell 2023. (Shixin Liu, Rockefeller University, New York, US)

Find more C-Trap publications

Publish more impactful science, faster 

Publish quickly and regularly in high impact journals.

Our customer are getting initial results within one week of their training, leading to publishing their first impactful studies in under 2 years.

Did you know, on average our C-Trap users are now publishing every 10 months? Not just that, but in journals with an average impact factor of 13!

Take the next step into uncovering unique molecular mechanisms

Download application notesTalk to an expert