Obtaining direct proof of the molecular mechanism of DNA-binding proteins

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:

Wasserman, M. et al.Replication Fork Activation Is Enabled by a Single-Stranded DNA Gate in CMG Helicase.Cell 2019, 178(3): 600-611.e616.
Khawaja, A. et al. Distinct pre-initiation steps in human mitochondrial translation. Nature Communications 2020, 11(1): 2932.

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

Source: www.lumicks.com/publications

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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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.”

Click here to watch the interview!

Professor at the University of Cambridge, Department of Biochemistry.

Prof. Pellegrini's group wants to understand how our cells execute the orderly duplication of the genome at the molecular level and how they cope with DNA damage. They aim to achieve their goal by working out the 3D shape of the protein complexes responsible for the duplication process, then using this information to explain their mechanism of action in atomic detail.

“We are extremely pleased to have received the generous support of the BBSRC (grant ref.MR/S021248/1) that enabled us to provide the University of Cambridge with a state-of-the-art single-molecule instrument that was not previously available to the Cambridge community of researchers. We are looking forward to the many novel insights that the C-trap will provide.”

Group leader and Professor of Physics of Living Systems at Vrije Universiteit Amsterdam.

An expert in protein structural dynamics, with a focus in single-molecule biophysics.

“I think that single-molecule has really [taught] us how molecular machines work, that has been the biggest breakthrough.”

Click here to watch the interview!

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.”

Click here to watch the interview!

Principal Scientist at the School of Life Sciences at Tsinghua University.

An expert in a combination of structural and functional approaches to resolving structures of RNA molecules and identify their functions and is a biologist who expanded into using dynamic single-molecule biophysics techniques to investigate the free energy related to RNA conformational changes.

“With the help of LUMICKS, my student started using this equipment after about 30 minutes of training [and] was quickly able to generate lots of data from it. I feel like this is going to be a very exciting tool in my lab that can help us to answer many important questions we have.”

Click here to watch the interview!

Download the on-demand webinar

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