06617
Octyl-α-D-glucopyranoside 100 mM solution
Synonym(s):
Octyl-α-D-glucopyranoside solution
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CAS Number:
UNSPSC Code:
12352201
storage temp.
2-8°C
InChI
1S/C14H28O6/c1-2-3-4-5-6-7-8-19-14-13(18)12(17)11(16)10(9-15)20-14/h10-18H,2-9H2,1H3/t10-,11-,12+,13-,14+/m1/s1
InChI key
HEGSGKPQLMEBJL-RGDJUOJXSA-N
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J D Doran et al.
Journal of pharmaceutical sciences, 101(1), 92-101 (2011-09-17)
Membrane proteins are attractive therapeutic targets, however the presence of detergents complicates biophysical binding measurements. Difficulties in determining quantitative dissociation constants for problematic membrane proteins were addressed by combining analytical ultracentrifugation and classical light scattering techniques. Validation of the algorithm
Matthew J Ranaghan et al.
The journal of physical chemistry. B, 114(44), 14064-14070 (2010-10-23)
The photochemical and thermal stability of the detergent-solubilized blue- and green-absorbing proteorhodpsins, BPR and GPR, respectively, are investigated to determine the viability of these proteins for photonic device applications. Photochemical stability is studied by using pulsed laser excitation and differential
Zahrabatoul Mosapour Kotena et al.
Journal of molecular modeling, 19(2), 589-599 (2012-09-14)
Density functional theory calculations on two glycosides, namely, n-octyl-β-D-glucopyranoside (C(8)O-β-Glc) and n-octyl-β-D-galactopyranoside (C(8)O-β-Gal) were performed for geometry optimization at the B3LYP/6-31G level. Both molecules are stereoisomers (epimers) differing only in the orientation of the hydroxyl group at the C4 position.
Kerry K Karukstis et al.
The journal of physical chemistry. B, 116(12), 3816-3822 (2012-03-06)
When mixed with water, n-octyl β-D-glucoside forms self-assembled nanostructures, several of which are liquid crystalline and all of which depend on the water/glucoside ratio and temperature. For practical use of these phases, a detailed understanding of the conditions under which
Alison Kan et al.
Journal of proteomics, 79, 299-304 (2012-12-04)
A high degree of optimisation is required in native co-immunoprecipitation (co-IP) experiments with added challenges for low-abundant membrane proteins and masking by IgG molecules. Although in vivo tagged-protein purification avoids the IgG masking problem, modifying the terminus of the protein
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