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Dodecyl-β-melibioside Detergent Micelles as a Medium for Membrane Proteins.
- Source :
-
Biochemistry [Biochemistry] 2017 Oct 17; Vol. 56 (41), pp. 5481-5484. Date of Electronic Publication: 2017 Oct 09. - Publication Year :
- 2017
-
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.
- Subjects :
- Amyloid beta-Protein Precursor chemistry
Detergents chemical synthesis
Diacylglycerol Kinase chemistry
Disaccharides chemical synthesis
Dynamic Light Scattering
Enzyme Stability
Escherichia coli Proteins chemistry
Glucosides chemistry
Glycolipids chemical synthesis
Hot Temperature adverse effects
Humans
Micelles
Myelin Proteins chemistry
Nuclear Magnetic Resonance, Biomolecular
Particle Size
Peptide Fragments chemistry
Peptide Fragments metabolism
Protein Interaction Domains and Motifs
Protein Stability
Receptor, Notch1 chemistry
Amyloid beta-Protein Precursor metabolism
Detergents chemistry
Diacylglycerol Kinase metabolism
Disaccharides chemistry
Escherichia coli Proteins metabolism
Glycolipids chemistry
Myelin Proteins metabolism
Receptor, Notch1 metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1520-4995
- Volume :
- 56
- Issue :
- 41
- Database :
- MEDLINE
- Journal :
- Biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 28980804
- Full Text :
- https://doi.org/10.1021/acs.biochem.7b00810