| Literature DB >> 28980804 |
James M Hutchison1, Zhenwei Lu1, Geoffrey C Li1, Benjamin Travis2, Ritesh Mittal2, Catherine L Deatherage1, Charles R Sanders1.
Abstract
There remains a need for new non-ionic detergents that are suitable for use in biochemical and biophysical studies of membrane proteins. Here we explore the properties of n-dodecyl-β-melibioside (β-DDMB) micelles as a medium for membrane proteins. Melibiose is d-galactose-α(1→6)-d-glucose. Light scattering showed the β-DDMB micelle to be roughly 30 kDa smaller than micelles formed by the commonly used n-dodecyl-β-maltoside (β-DDM). β-DDMB stabilized diacylglycerol kinase (DAGK) against thermal inactivation. Moreover, activity assays conducted using aliquots of DAGK purified into β-DDMB yielded activities that were 40% higher than those of DAGK purified into β-DDM. β-DDMB yielded similar or better TROSY-HSQC NMR spectra for two single-pass membrane proteins and the tetraspan membrane protein peripheral myelin protein 22. β-DDMB appears be a useful addition to the toolbox of non-ionic detergents available for membrane protein research.Entities:
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Year: 2017 PMID: 28980804 PMCID: PMC5685800 DOI: 10.1021/acs.biochem.7b00810
Source DB: PubMed Journal: Biochemistry ISSN: 0006-2960 Impact factor: 3.162