title: High throughput methods of assessing protein stability and aggregation.
abstract: 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).
authors.affiliation: Structural Genomics Consortium, Suite 700, 7th Floor, MaRS South Tower, 101 College St., Toronto, ON M51L7, Canada. g.senisterra@utoronto.ca
authors.forename: Guillermo A
authors.initials: GA
authors.lastname: Senisterra
authors.forename: Patrick J
authors.initials: PJ
authors.lastname: Finerty
mesh_terms: D001671:Biochemistry / Q000379:methods*; D006801:Humans; D008027:Light; D011489:Protein Denaturation; D055550:Protein Stability; D020836:Protein Structure, Quaternary; D012542:Scattering, Radiation