Protein Stability

Knowing the aggregation state of a protein is of crucial importance. Whether finding the optimal conditions for long-term storage or performing a basic physicochemical characterization, ProbeDrum is the ultimate tool box to conveniently track your sample.

The multiple readout options of ProbeDrum provide different windows into protein stability. Changes in RALS can give information about changes in size, from oligomerization to precipitation. Fluorescence allows monitoring of changes in intrinsic fluorescence which can report on the folding state of proteins. Adding reporter dyes to the sample, such as ANS or ThT, expands the possibilities even further. 

Long term stability

Proteins can often exist in a meta-stable state, where they appear stable in the short term but will aggregate over a longer time. In ProbeDrum it is very easy to monitor protein long term stability by recording light scattering or fluorescence signals at set intervals over time. An interesting special case of this is amyloid proteins, known for their propensity to aggregate into fibrils. Amyloid aggregation kinetics can be obtained using a combination of light scattering and a fluorescent reporter dye.

pH stability

pH has a significant impact on protein stability, folding state, and function. ProbeDrum makes it easy to get the full picture of these often complex interactions. With the automated titrations system and the ability to get direct feedback from a pH electrode the pH-dependent behavior of a protein can be mapped in high detail and accuracy. 

Thermal Stability

Determining thermal stability is a cornerstone of protein characterization. With ProbeDrum this can conveniently be automated and by directly controlling the temperature of the sample the accuracy of the temperature can be assured.

Automate and refine. Remove tedious, repetitive labor. Free up time for science!