Biomolecules, such as RNA, DNA, proteins and polysaccharides, are at the heart of fundamental cellular processes. These molecules differ greatly with each other in terms of their structures and functions. However, in the midst of the diversity of biomolecules is the unifying feature that they interact with each other to execute a viable biological system. Interactions of biomolecules are critical for cells to survive and replicate, for food metabolism to produce energy, for antibiotics and vaccines to function, for spreading of diseases and for every other biological process. An improved understanding of these interactions is crucial for studying how cells and organs function, to appreciate how diseases are caused and how infections occur, with infinite implications in medicine and therapy. Many biochemical and biophysical techniques are currently being employed to study biomolecular interactions. Microscale thermophoresis (MST) is a relatively new biophysical technique that can provide powerful insight into the interactions of biomolecules and is quickly being adopted by an increasing number of researchers worldwide. This article provides a brief description of principles underpinning the MST process, in addition to benefits and limitations.
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Feature| April 01 2019
Microscale thermophoresis: warming up to a new biomolecular interaction technique
Tyler Mrozowich ;
Vanessa MeierStephenson ;
Biochem (Lond) (2019) 41 (2): 8–12.
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Tyler Mrozowich, Vanessa MeierStephenson, Trushar R. Patel; Microscale thermophoresis: warming up to a new biomolecular interaction technique. Biochem (Lond) 1 April 2019; 41 (2): 8–12. doi: https://doi.org/10.1042/BIO04102008
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