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).

journal_name

Mol Biosyst

journal_title

Molecular bioSystems

authors

Senisterra GA,Finerty PJ Jr

doi

10.1039/b814377c

subject

Has Abstract

pub_date

2009-03-01 00:00:00

pages

217-23

issue

3

eissn

1742-206X

issn

1742-2051

journal_volume

5

pub_type

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