Call for research proposals

Dynamic single-molecule investigation of coronavirus structure and function

Our dedication to bettering human health starts by collaborating with you to expand the research on coronaviruses further. In the coming months, we will commit part of our in-house capacity and single-molecule expertise to accept your samples and conduct proof-of-concept experiments.

If you have a single-molecule assay related to the coronavirus or COVID-19 in mind, please join us in this endeavor by submitting your research proposal!


Together we can study:

– Kinetics and energy landscapes associated with conformational changes of viral proteins, such as SPIKE.
– Packaging of viral DNA or RNA.
– Autoregulation of viral translation.
– Interactions between viral DNA or RNA and capsid proteins, or between a virus and the host cell.
– Protein-induced viral shedding and fusion.

Terms & Conditions

Instrument configuration: dual trap optical tweezers with 3-colour confocal fluorescence.

-No access to facilities with biosafety certification.

-Only experiments for fundamental research on SARS-CoV-2 associated processes.

-We will accept and test samples for free to generate proof data.

-Experiments will be selected and scheduled based on research proposal and priority.

Get in touch!

See how it’s possible to study viruses using LUMICKS technologies

Record the interaction forces between a virus and the host cell

You can use the C-Trap to investigate the dynamic interactions between a single virus and the cell surface receptors of a host cell. This approach enables you to direct an optically-trapped bead, coated with your virus of interest, towards adherent cells. Subsequently, you can push the bead against the cell membrane and pull it away after contact. The pulling force required to disrupt the established interactions between the virus and host cell indicates the strength of the interaction. Read more…

Establish the kinetics and energy landscapes associated with conformational changes of viral proteins

With optical tweezers instruments like the C-Trap, you can attach the ends of a viral protein between two beads, apply mechanical force to unfold the protein, and investigate the related kinetics. By studying these features at the single-molecule level, you can probe the intermediate conformations, a crucial detail that is commonly missed by other conventional methods. This kind of assay can, for example, provide you insights into how specific drugs disrupt viral proteins and their conformational dynamics during infections. Read more…

C-Trap Protein Folding

Manipulate and visualize the autoregulation of viral RNA translation

RNA pseudoknots are secondary structures of RNA that are critical in autoregulating translation and ribosomal frameshifting in many virus types. The C-Trap offers you the means to study the structural dynamics of RNA pseudoknots at the single-molecule level to reveal how secondary and tertiary RNA conformations regulate viral translation. By creating and stretching a so-called dumbbell system including an RNA and two trapped beads, you can investigate forces associated with each step of structure unfolding and folding. Read more…

Time and quantify packaging of viral DNA

Using optical tweezers, you can study the processes by which viruses pack large amounts of genetic material in confined environments and uncover critical steps and requirements in viral DNA packaging. For example, you can tether a DNA packaging motor and one end of the DNA substrate between two optically trapped beads. Next, you can directly measure distance changes between the two trapped beads during DNA packaging. Both the cycle duration (period of fast packaging and pause) and the amount of packed DNA reveal the functions of the specific motor.  Read more…

Measure and visualize interactions between viral DNA and capsid proteins

Using optical tweezers correlated with fluorescence microscopy, you can study the nucleation and growth process of viral particles while capsid proteins interact with nucleic acids. For instance, the C-Trap can tether a double-stranded DNA between two beads and subsequently expose the single molecule to viral capsid proteins. As these proteins bind to the DNA, they shorten the nucleic acid through compaction. The fluorescently labeled capsid proteins reveal progressively compacted protein–DNA complexes as the fluorescence intensity increases. Read more…

C-Trap DNA-Protein Interactions General

Investigate and monitor protein-induced viral shedding and fusion

Optical tweezers are optimal to simultaneously apply and measure forces associated with membrane deformation upon viral shedding. The fluorescence imaging provided in the C-Trap further enables you to visualize the curvature of the host cell’s membrane as well as the distribution of labeled membrane proteins while simultaneously assessing the forces associated with shedding. The approach is unique in that it reveals the relationship between membrane curvature and viral proteins during budding, which can be correlated with its shedding efficiency. Read more…

Detect and select viral particles in a contact-free manner

While, in most cases, virus particles are small and aggregate in liquids which may confound the intended measurements, optical tweezers enable you to catch virus particles in solution and differentiate single particles from aggregates. The optical trapping of a single virus particle enables you to control its location. On top of that, you can fluorescently label viral membrane proteins and quantify them based on fluorescence intensity in order to correlate protein levels with your desired measurements. Read more…

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