×

Sign up to receive
the latest NanoTemper news, product updates, event announcements and more

First Name
Last Name
Company Name
Country
State
Province
State
Region
State
Canton
Agree to Subscribe & Privacy Policy*
*I have fully read, understood and agree to the Privacy Policy. I accept the storing and processing of my personal data by NanoTemper as described in the Privacy Policy.

By completing this form, you provide us consent to contact you with educational content, news and information about our products, services and events. You may unsubscribe at any time.
Thank you!
Error - something went wrong!
   

What binding affinity and binding kinetics tell you about protein-ligand interactions

What measurements are most important for studying how proteins interact? The answer depends on your research needs. There is debate about which is more important: measuring how fast and specific the interaction is between two biomolecules (binding kinetics), or the strength between them (binding affinity). Real-time measurements like surface plasmon resonance (SPR) provide binding affinity and kinetics, but does that mean researchers always need it? Delving into the differences in protein measurement types and current instrument technologies can help you determine which one will best serve your research purposes.

Previous
Protein labeling – improved quantitation of biomolecular interactions by MST using the His-Tag labeling kit RED-tris-NTA 2nd generation
Protein labeling – improved quantitation of biomolecular interactions by MST using the His-Tag labeling kit RED-tris-NTA 2nd generation

Up next
The why, what and when of binding affinity
The why, what and when of binding affinity

Have a question about Monolith?

Contact Specialist