Interhelical Packing in Detergent Micelles
نویسندگان
چکیده
منابع مشابه
Molecular Packing in Cylindrical Micelles
The elongated shape of linear, worm-like, micelles is among the most common aggregation geometries of amphiphilic molecules in aqueous solutions. The cylindrical body of these uni-dimensional micelles can be regarded as an intermediate packing geometry, of a higher growth dimensionality than that of a spherical micelle and lower than that of a planar bilayer. In all these three canonical struct...
متن کاملStructure of DNA-cationic liposome complexes: DNA intercalation in multilamellar membranes in distinct interhelical packing regimes.
Cationic liposomes complexed with DNA (CL-DNA) are promising synthetically based nonviral carriers of DNA vectors for gene therapy. The solution structure of CL-DNA complexes was probed on length scales from subnanometer to micrometer by synchrotron x-ray diffraction and optical microscopy. The addition of either linear lambda-phage or plasmid DNA to CLs resulted in an unexpected topological tr...
متن کاملGrowth of Sodium Dodecyl Sulfate Micelles with Detergent Concentration
Sodium alkyl sulfate micelles are predicted to grow as a power law of the total counterion salt concentration, Yaq, in the aqueous phase as follows: NA = K~(Y~~)Y, where N A is the micelle aggregation number and ~2 and y are constants which are estimated from the critical micelle concentration and the apparent degree of counterion attachment. For sodium dodecyl sulfate, NA = 162(Y,q)1/4 is pred...
متن کاملDetergent-phospholipid mixed micelles with a crystalline phospholipid core.
An unusual micelle was discovered in mixtures of the nonionic detergent octaethyleneglycol-mono-n-dodecylether with disaturated phospholipids such as 1,2-dimyristoyl-sn-glycero-3-phosphocholine or 1,2-dipalmitoyl-sn-glycero-3-phosphocholine in water. These mixtures undergo a structural transition upon cooling through the chain-melting temperatures of the respective phospholipids, resulting in t...
متن کاملOuter membrane protein A of E. coli folds into detergent micelles, but not in the presence of monomeric detergent.
Outer membrane protein A (OmpA) of Escherichia coli is a beta-barrel membrane protein that unfolds in 8 M urea to a random coil. OmpA refolds upon urea dilution in the presence of certain detergents or lipids. To examine the minimal requirements for secondary and tertiary structure formation in beta-barrel membrane proteins, folding of OmpA was studied as a function of the hydrophobic chain len...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2002
ISSN: 0021-9258
DOI: 10.1074/jbc.m110264200