Binding Kinetics Simulator
Resource
Interactive CMI Tool to simulate binding kinetics and model surface-based kinetic binding experiments, such as Surface Plasmon Resonance and Biolayer Interferometry.
molecular interactions
Content tagged with molecular interactions
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Measuring Molecular Interactions
Page
A wide array of biomolecular interactions from protein/protein interactions to small molecule ligand/compound binding interactions are important in biology. Fundamentally, there are two ways to measure (or quantify) binding of any of these interactions...
May I collect data during training?
FAQ
We do NOT collect User Data during CMI training sessions.
All Training sessions include:
- Overview of the instrument and maintenance procedures
- Tutorial on control and analysis software
- Review of experimental design
- User trainings may be individual or small...
I want to measure a Kd, how do I choose which technique is best?
FAQ
The CMI has four primary technologies to quantify molecular interactions: Surface Plasmon Resonance (SPR) and Biolayer Interferometry (BLI), Isothermal Titration Calorimetry (ITC) and MicroScale Thermophoresis (MST). Each technologies has its advantages...
Where do I get supplies? *
FAQ
Most specialized instrument supplies and reagents will be purchased by the user directly from the vendor
Including:
- BLI: Sartorius Biosensors
- SPR: Cytiva Sensor Chips (Biacore SERIES S)
- SPR: Cytiva Immobilization reagents
- MP: Refeyn pre-cleaned cover slides
- Nan...
To measure a molecular interaction, how do you choose which molecule to be kept at a fixed concentration and which to vary in concentration?
FAQ
The choice of which molecule to keep constant and which to vary will depend on the experiment type, the properties of the molecules and the stoichiometry of the interaction.
For ITC, where neither protein is labeled or immobilized, either molecule can be...
How much sample is needed for a binding assay?
FAQ
The amount (volume and concentration) of sample that you need will vary by method and by the Kd (equilibrium dissociation constant) of the interaction. For guidelines see the CMI technology comparison table. Binding assays will typically have one...
For a kinetic binding assay using Surface Plasmon Resonance (SPR) or Biolayer Interferometry (BLI), how do I chose which of my binding partners to immobilize?
FAQ
The relative size of the molecules isn't generally the deciding factor. Large proteins will typically give larger signals, but that isn’t necessarily better.
For protein/protein interactions, start by considering other properties of the proteins. Most...
For a binding assay using MicroScale Thermophoresis (MST), which binding partner should be fluorescently labeled?
FAQ
MST experiments on the Monolith NT.115 pico require that one of the binding partners is fluorescently labeled.
For protein/protein interactions, start by considering the amounts, solubility and sequence of the proteins. The labeled target is typically...