Dodecyl-ß-melibioside Detergent Micelles as a Medium for Membrane Proteins.
Biochemistry
; 56(41): 5481-5484, 2017 10 17.
Article
em En
| MEDLINE
| ID: mdl-28980804
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-ß-melibioside (ß-DDMB) micelles as a medium for membrane proteins. Melibiose is d-galactose-α(1â6)-d-glucose. Light scattering showed the ß-DDMB micelle to be roughly 30 kDa smaller than micelles formed by the commonly used n-dodecyl-ß-maltoside (ß-DDM). ß-DDMB stabilized diacylglycerol kinase (DAGK) against thermal inactivation. Moreover, activity assays conducted using aliquots of DAGK purified into ß-DDMB yielded activities that were 40% higher than those of DAGK purified into ß-DDM. ß-DDMB yielded similar or better TROSY-HSQC NMR spectra for two single-pass membrane proteins and the tetraspan membrane protein peripheral myelin protein 22. ß-DDMB appears be a useful addition to the toolbox of non-ionic detergents available for membrane protein research.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Glicolipídeos
/
Precursor de Proteína beta-Amiloide
/
Diacilglicerol Quinase
/
Proteínas de Escherichia coli
/
Detergentes
/
Dissacarídeos
/
Receptor Notch1
/
Proteínas da Mielina
Limite:
Humans
Idioma:
En
Ano de publicação:
2017
Tipo de documento:
Article