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Methods. 2011 Dec;55(4):324-9. doi: 10.1016/j.ymeth.2011.07.008. Epub 2011 Aug 5.

Simple screening method for improving membrane protein thermostability.

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1
The Helen L. and Martin S. Kimmel Center for Biology and Medicine at the Skirball Institute of Biomolecular Medicine, Department of Cell Biology, New York University School of Medicine, 540 First Avenue, New York, NY 10016, USA.

Abstract

Biochemical and biophysical analysis on integral membrane proteins often requires monodisperse and stable protein samples. Here we describe a method to characterize protein thermostability by measuring its melting temperature in detergent using analytical size-exclusion chromatography. This quantitative method can be used to screen for compounds and conditions that stabilize the protein. With this technique we were able to assess and improve the thermostability of several membrane proteins. These conditions were in turn used to assist purification, to identify protein ligand and to improve crystal quality.

PMID:
21840396
PMCID:
PMC3220791
DOI:
10.1016/j.ymeth.2011.07.008
[Indexed for MEDLINE]
Free PMC Article

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