Reveal the structural dynamics of RNA & DNA in real time

Use Dynamic Single-Molecule to obtain the full understanding of DNA/RNA structure
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Dynamic Single-Molecule

Revealing biomolecular insights never before available

Dynamic Single-Molecule page
Why Dynamic Single-Molecule?

Redefine nucleic acids research and observe every conformational change at the single-molecule level

The dynamic structures of RNA and DNA molecules underpin essential biological mechanisms in health and disease, directly influencing viral replication, cancer pathways, and neurodegeneration. Understanding these structural dynamics drives innovative therapeutic development. However, conventional biophysical approaches average signals over millions of molecules, obscuring crucial short-lived intermediate states and providing limited kinetic information. As a result, true structural dynamics insights of disease-relevant nucleic acids remain elusive.
Overcome these challenges with Dynamic Single-Molecule technology through:
  • Observe individual RNA or DNA molecules transitioning in real time among folded, misfolded, and intermediate conformations
  • Reveal how proteins, ligands, drugs or sequence elements reshape nucleic acid folding and structure landscapes
  • Quantify structural, kinetic, and energy landscape parameters—even for highly complex RNA molecules

Uncover structural dynamics in telomeric RNA for cancer research

G-quadruplexes are specialized DNA and RNA structures that form in guanine-rich regions critical for telomere integrity and cellular aging. These dynamic structures regulate gene expression and chromosome stability, with disruption implicated in cancer development and aging-related diseases. Despite extensive study, scientists cannot directly observe how G-quadruplexes fold and function in real biological contexts—limiting our ability to target them therapeutically. With cancer affecting millions worldwide, understanding these structures has become essential for developing novel targeted treatments.

Case study

Revealing stability and dynamics of telomeric G-quadruplexes

Bo Sun, PhD
Associate Professor

A study led by Bo Sun at ShanghaiTech University explored how human telomerase RNA (hTR) forms and maintains stable G-quadruplex structures. Using LUMICKS C-Trap, they monitored real-time folding and unfolding of single hTR molecules, revealing:

  • Multiple distinct G-quadruplex conformations exist, identifiable only by single-molecule force spectroscopy.
  • Local RNA sequences strongly modulate the unfolding and refolding kinetics of these critical telomeric structures.
  • These novel insights into G4 structural dynamics offer novel therapeutic strategies for targeting telomere-related diseases, including cancers and aging.

Reference:

Ye et al., The Journal of Physical Chemistry Letters (2021).
Prof. Bo Sun Lab - ShanghaiTech University
“Proximal Single-Stranded RNA Destabilizes Human Telomerase RNA G‑Quadruplex and Induces Its Distinct Conformers.”

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Investigate RNA misfolding in neurodegenerative disorders

Expanded repeat sequences in RNA form abnormal structures linked to numerous neurodegenerative diseases including Huntington's, ALS, and certain ataxias. These toxic RNA structures aggregate in cells and disrupt normal neuronal function, triggering progressive neurodegeneration. Despite significant advances in genetic diagnosis, researchers cannot visualize how these repeat expansions actually misfold and aggregate —hampering therapeutic development. With neurodegenerative disorders affecting over 50 million people globally, understanding RNA structural dynamics has become critical for developing effective treatments.

Case study

Elucidating toxic RNA misfolding dynamics in Huntington’s disease

Christian Kaiser, PhD
Professor

Researchers Christian Kaiser and Sarah Woodson at Johns Hopkins University investigated how expanded CAG repeats in HTT mRNA influence misfolding and aggregation. By applying real-time single-molecule force measurements with LUMICKS C-Trap, they discovered:

  • Healthy (normal) HTT mRNA unfolds cooperatively in a single well-defined step.
  • Expanded repeats unfold stepwise (“stick-slip” pattern) at lower forces, indicating non-cooperative behavior.
  • Frequent partially unfolded structures self-associate, directly linking RNA misfolding dynamics to Huntington disease progression

Reference:

O’Brien et al., Nature Communications (2024).Prof. Christian Kaiser and Prof. Sarah Woodson - Johns Hopkins University“Stick-slip unfolding favors self-association of expanded HTT mRNA.”

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Reveal protein-RNA interactions critical for viral replication

RNA pseudoknots are complex folded structures that regulate critical processes in viral replication and gene expression. These dynamic elements enable viruses to produce multiple proteins from limited genetic material and evade host defenses through conformational changes. Despite their central role in viral pathogenesis, scientists cannot directly observe how these structures interact with host proteins during infection—limiting antiviral development. With viral diseases continuously threatening global health security, understanding RNA structural dynamics has become essential for creating next-generation antivirals.

Case study

Protein-mediated frameshift regulation in SARS-CoV-2

Neva Caliskan, PhD
Group Leader

A study led by the Neva Caliskan Lab at the Helmholtz Institute for RNA-Based Infection Research investigated how ZAP-S protein modulates SARS-CoV-2 frameshifting through altering the pseudoknot structure. By directly tracking the real-time pseudoknot structural dynamics in the presence or absence of ZAP-S using LUMICKS C-Trap, they revealed:

  • ZAP-S binding destabilizes the mRNA pseudoknot structure, preventing its refolding and impairing frameshifting activity essential for viral protein production.
  • Reduced frameshifting efficiency means fewer essential viral proteins are produced, weakening the virus’s ability to replicate.
  • Ultimately, viral replication is significantly reduced, highlighting ZAP-S interaction with the pseudoknot as a novel, targetable antiviral mechanism with clear translational potential.

Reference:

Zimmer et al., Nature Communications (2021).Prof. Neva Caliskan - Helmholtz Institute for RNA-Based Infection Research“The short isoform of the host antiviral protein ZAP acts as an inhibitor of SARS-CoV-2 programmed ribosomal frameshifting.”

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Discover novel mechanisms driving antibiotic resistance

Bacterial integrons are genetic elements that enable bacteria to capture external genes and develop antibiotic resistance. These molecular machines incorporate resistance genes through DNA recombination, driving the spread of untreatable infections. Despite decades of research, scientists still cannot explain why some genes transfer efficiently while others don't—a critical gap hindering our ability to predict resistance spread. With resistant infections causing over 1.2 million deaths annually, understanding these mechanisms has become urgent.

Case study

A novel targetable mechanism against antibiotic resistance: the structural stability of bacterial integrons

Michael Schlierf, PhD
Group Leader

A breakthrough study led by Michael Schlierf at TU Dresden in collaboration with Didier Mazel at Institut Pasteur investigated this mystery using single-molecule techniques. By applying controlled forces to individual DNA-IntI1 integrase complexes with LUMICKS C-Trap, they revealed:

  • Efficiently recombining DNA sites form mechanically stable complexes with the IntI1 protein that resist forces up to high forces.
  • Poorly recombining DNA sites form weaker protein-DNA complexes that break apart at lower forces.
  • The mechanical stability of these IntI1-DNA complexes directly correlates with recombination efficiency in living bacteria, revealing a physical basis for genetic adaptation and a potential target for combating antibiotic resistance.

Reference: Vorobevskaia et al., Science Advances (2024). Prof. Michael Schlierf Lab - TU Dresden & Prof. Didier Mazel Lab - Institut Pasteur "The recombination efficiency of the bacterial integron depends on the mechanical stability of the synaptic complex."

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Solutions

C-Trap

Biomolecular interactions re-imagined

The C-Trap® provides the world’s first dynamic single-molecule microscope to allow simultaneous manipulation and visualization of single-molecule interactions in real time.

Discover the C-Trap

Publications

Understand the key insights by reading up on our latest publications

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Text Link

Proximal Single-Stranded RNA Destabilizes Human Telomerase RNA G-Quadruplex and Induces Its Distinct Conformers

Ye, S. et al.
2021
J. Phys. Chem. Lett.
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DNA/RNA Structure
Publication

Relevant resources

Learn as much as you can by reading up on our application notes or marathoning our webinars.

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Unveiling Key Mechanisms in Kinetochore-Mediated Chromosome Segregation with the C-Trap

Unveiling Key Mechanisms in Kinetochore-Mediated Chromosome Segregation with the C-Trap

Scientific update
Chenlu Yu, PhD

DNA-Binding proteins

DNA Editing

DNA/RNA Structure

DNA Organization

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Deciphering the structure–function relationship of RNA - a complete guide

Deciphering the structure–function relationship of RNA - a complete guide

Application note
01-01-20
01-01-20

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SITC 2025

SITC 2025

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April 22, 2025
01-01-20

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CICON 2025

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