Jump to main content
Jump to site search

Issue 3, 2009
Previous Article Next Article

High throughput methods of assessing protein stability and aggregation

Author affiliations

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).

Graphical abstract: High throughput methods of assessing protein stability and aggregation

Back to tab navigation

Publication details

The article was received on 21 Aug 2008, accepted on 04 Nov 2008 and first published on 24 Dec 2008


Article type: Review Article
DOI: 10.1039/B814377C
Mol. BioSyst., 2009,5, 217-223

  •   Request permissions

    High throughput methods of assessing protein stability and aggregation

    G. A. Senisterra and P. J. Finerty, Jr, Mol. BioSyst., 2009, 5, 217
    DOI: 10.1039/B814377C

Search articles by author

Spotlight

Advertisements