Proteins were discovered in the late eighteenth century, but it wasn’t until over a hundred years later that the first tools to analyse them were developed. Many of these early analysis tools are still routinely used in modern biochemical analysis laboratories — albeit with many improvements.
For example analytical ultracentrifugation (AUC) was invented in 1923 by the Swedish chemist and Nobel laureate Theodor Svedberg, and is still in heavy use – Google Scholar shows over 25,000 results for just the last 3 years!
The scientific principles behind many of these techniques had been known for many years prior to their utilization in protein analysis, and it is only comparatively recently that instruments capable of exploiting these principles have been developed. For example, the first dynamic light scattering (DLS) instrumentation became available in the 1970s; however, Brownian motion, one of the core principles behind this technique — which explains how the movement of molecules in a solution is proportional to their size — was first proposed by Albert Einstein in 1905.
In addition to increasing the breadth of proteins that can be analyzed, modern protein sizing technologies provide much faster access to results with lower sample input requirements. For example, microfluidic diffusional sizing (MDS) enables accurate protein sizing and quantification using 50 ng of sample. This compares extremely favorably to AUC, which can require around 50 µg. Like AUC, MDS also allows analysis of proteins in their native buffer composition/formulation.
More information about protein analysis techniques, including their advantages and limitations, can be found in our recent resources below.