RSC Publishing


Publishing

 

Cover image for Molecular BioSystems, select for current issue

Molecular BioSystems

Research at the interface between chemistry and the -omic sciences and systems biology.



Subscribers

  • PDF
  • HTML article

Non-subscribers

Free access



Review

Mol. BioSyst., 2009, 5, 217 - 223, DOI: 10.1039/b814377c


High throughput methods of assessing protein stability and aggregation

Guillermo A. Senisterra, Patrick J. Finerty and Jr


The significant increase in the demand for purified protein for crystallization and structural studies has made necessary the development of multi-sample methods for identifying solution conditions that affect protein stability and aggregation. Conditions that stabilize proteins can improve protein purification and crystallization. These methods can be used to identify small molecule compounds or inhibitors that interact with the purified proteins, and might serve as starting points for drug discovery. In this article three methods for measuring protein stability and aggregation are described and discussed: differential scanning fluorimetry (DSF), differential static light scattering (DSLS), and isothermal denaturation (ITD).

Graphical abstract image for this article  (ID: b814377c)