期刊
METHODS
卷 55, 期 4, 页码 324-329出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.ymeth.2011.07.008
关键词
Membrane proteins; Size exclusion chromatography; Protein thermostability
资金
- American Heart Association
- NIH [HL091618, AI086072]
- NIDDK [DK053973-08A1S2]
- Protein Structure Initiative II of the National Institutes of Health [GM075026]
- National Institutes of Health [DK073973, MH083840, GM093825]
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. (C) 2011 Elsevier Inc. All rights reserved.
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