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Our hypothesis was that, in the case of large biomolecules, the changes of molecular conformation caused by the pressure or high flow rates (thermal effects) will play a much more important role in changing retention and selectivity. Especially when considering their “bind and elute” type retention behavior. In our work, this huge conformational change was experimentally verified both by fluorescence emission measurements and by the analysis of native and reduced forms of various proteins which possess the same molecular weight but a different conformation.
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First, Giddings showed that increased pressure could induce significant changes in molecular volume and the ability of molecules to crowd together to reduce molecular volume upon adsorption. Later on, Guiochon and McCalley reported interesting results observed in isocratic mode and mostly for small-molecule separations. However, the change in retention and selectivity caused by pressure was relatively minor when eluting small solutes (in the pressure range up to 1000 bar).
We are also involved in the development of new column designs and stationary phases which we believe will change the current practice of protein chromatography.
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Mk Usmaan is an avid AI enthusiast who studies and writes about the latest developments in artificial intelligence. As an aspiring computer scientist, he is fascinated by neural networks, machine learning, and how AI technology is rapidly evolving.
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