In kinetics there seems to be a race for the best (lowest in this context) equilibrium dissociation constant (K_D) there is. Interactions are compared by their equilibrium dissociation constant and that is it. Similarly often only the IC50 of a system is given while the full kinetics are not well established.

In my opinion, reporting a single value for a kinetic interaction is hiding all the other information present in the measurements between two or more components.

With regular maintenance your instrument is in perfect order. In addition you make the best, clean and degassed buffers. But what about the proteins you use? Are they of the best quality? And this new batch is the same as the previous, you are sure of that?
Is your protein affected by the buffer and immobilization conditions used? Your assay problems might be caused by poor protein quality!
Luckily there is an easy and fast way to check the integrity of your proteins. Nanotemper Technologies provides various instruments to check your protein quality, all using a minimum of sample. .

Surface Plasmon Resonance (SPR) seems to be difficult for many people. Judging on the literature many of you are struggling to get nice sensorgrams with easy to fit curves. However, SPR is straightforward when you know what you are doing. Consequently, you have to learn how SPR works, how to perform an experiment and how to analyze it. So what are the key parts of a proper SPR experiment?

Ryan Denomme of Nicoya publishes a nice blog about SPR and related topics. For instance about preserving precious sample by optimizing preconcentration and immobilization or what the difference is between SPR and LSPR.
Definitely worthwhile to check this blog!

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