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.
Most recent content
Why Dr. Elsa Wagner from Pierre Fabre chose Prometheus Panta for mAbs developability assessment
Read why scientist Dr. Elsa Wagner chose the Prometheus Panta instrument with simultaneous measurements of DLS, nanoDSF, SLS and backreflection for developability assessment of their mAbs candidates.
The biologics researcher's mini-guide to screening candidates with nanoDSF
Read this nanoDSF guide to learn how nano-Differential Scanning Fluorimetry (nanoDSF) uses your protein’s intrinsic fluorescence to determine its melting temperature, Tm and onset of melting, Ton.
Use this downloadable list of 2023 Targeted Protein Degradation conferences to choose which one(s) to attend. Learn when and where they’ll happen, who’ll be there, and the main focus.
Use this downloadable list of 2023 biologics conferences to select which one to attend. Learn when and where they’ll happen, who’ll be there, and the main focus.
Advance your understanding of neurodegenerative diseases
Use this eBook to advance your own neurodegenerative diseases (ND) research by reading a selection of peer-reviewed publications. Find out how researchers are gaining insight into the molecular mechan