Journal of oleo science, 60(5), 229-236 (2011-04-20)
The secondary structure of bovine serum albumin (BSA) in the binary surfactant system of anionic sodium dodecyl sulfate (SDS) and zwitterionic N-dodecyl-N,N-dimethyl-3-ammonio-1-propanesulfonate (DDAPS) was examined at 25°C. The helicity of BSA decreased from 66% to 55% in a solution of
Inositol 1,4,5-trisphosphate receptors (IP(3)Rs) are a family of intracellular Ca(2+) channels that exist as homo- or heterotetramers. In order to determine whether the N-terminal ligand-binding domain is in close physical proximity to the C-terminal pore domain, we prepared microsomal membranes
European journal of biochemistry, 269(21), 5215-5223 (2002-10-24)
Opacity-associated (Opa) proteins are outer membrane proteins which play a critical role in the adhesion of pathogenic Neisseria spp. to epithelial and endothelial cells and polymorphonuclear neutrophils. The adherence is mainly mediated by the CD66-epitope-containing members of the carcinoembryonic-antigen family
Langmuir : the ACS journal of surfaces and colloids, 20(25), 10858-10867 (2004-12-01)
Micellization in sodium dodecyl sulfate (SDS)-N-dodecyl-N,N-dimethyl-3-ammonio-1-propanesulfonate and SDS-polyoxyethylenesorbitan monolaurate binary surfactant solutions was studied by means of conductivity and surface tension measurements. These studies showed that two types of micellar aggregates are present in the mixed micellar solutions. Two reactions
