Below are a links to various studies biological and chemistry, where dodecyl maltoside or other maltoside detergents were used:
- A 1999 study published in The Journal of Biological Chemistry shows NhaA Antiporter activity in E. Coli is the result of a conformational change dependent on pH. Specifically involves Lys-249 residue and NhaA Antiporter transmembrane segments VIII and IX.
- A paper published in 1986 in Biochimica et Biophysica Acta (BBA) - Biomembranes, discusses the differences in alkyl chain structures of various maltoside detergents and their effect on dialysis kinetics and liposome formation.
- Journal of Biological Chemistry, 1994 a study (fluorescence spectroscopy) on light-dependent activation of the Rhodopsin protein and its decay. The activity of this protein was studied in a 0.1% dodecyl maltoside solution. What was the pH of the solution? 6.0.
- Insight into the physical chemistry and physics of foam films formed by detergents. The study is based in the DLVO theory and provides evidence that demonstrates the existence of electrical charges at the at the interface of water-surfactant and goes further to quantify the charge density. This study was published in the journal of Physical Chemistry Chemical Physics (2002).
- High Resolution Structure of Cytochrome C. This study shows specific amino acid residues where lipids and detergents bind. The results have been proven to be reproducible. The detergents used in this study are maltosides. The study was performed by the California Institute of Technology in 2006.
- A transmembrane study involving replacement mutations of highly conserved residues in bovine rhodospin. The study then studies the activity of these mutated protein was and compared to the wild-type. The amino acids involved are phenylalanine, alanine and gylcine. The study was published in 1996 and was conducted by the Howard Hughes Medical Institute. Find the abstract here.
Find physical and chemical proprieties of dodecyl maltoside
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