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).
journal_name
Mol Biosystjournal_title
Molecular bioSystemsauthors
Senisterra GA,Finerty PJ Jrdoi
10.1039/b814377csubject
Has Abstractpub_date
2009-03-01 00:00:00pages
217-23issue
3eissn
1742-206Xissn
1742-2051journal_volume
5pub_type
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