Biliquid oil-in-water nanofoams and spontaneous emulsification obtained with a surfactant resistant to curvature changes.

Hypothesis: Due to its huge polar headgroup, octaoxyethylene octyl ether carboxylic acid (CECHCOOH = Akypo LF2™) is supposed not to be able to change its curvature sufficiently to form bicontinuous microemulsions. Instead, upon adding an oil to the binary water - surfactant system, excess oil could be squeezed out or a biliquid foam could form.

Experiments: An auto-dilution setup was used to record small-angle X-ray scattering data along six dilution lines in the newly established phase diagram of the ternary system 2-ethylhexanol - CECHCOOH - water.

Determination of absolute intramolecular distances in proteins using anomalous X-ray scattering interferometry.

Biomolecular structures are typically determined using frozen or crystalline samples. Measurement of intramolecular distances in solution can provide additional insights into conformational heterogeneity and dynamics of biological macromolecules and their complexes. The established molecular ruler techniques used for this (NMR, FRET, and EPR) are, however, limited in their dynamic range and require model assumptions to determine absolute distance or distance distributions.

Sarcomere, troponin, and myosin X-ray diffraction signals can be resolved in single cardiomyocytes.

Cardiac function relies on the autonomous molecular contraction mechanisms in the ventricular wall. Contraction is driven by ordered motor proteins acting in parallel to generate a macroscopic force. The averaged structure can be investigated by diffraction from model tissues such as trabecular and papillary cardiac muscle using collimated synchrotron beams, offering high resolution in reciprocal space.

Two populations of protein molecules detected by small-angle neutron and X-ray scattering (SANS and SAXS) in lyophilized protein:lyoprotector (disaccharide) systems.

Two protein interaction peaks are observed in pharmaceutically-relevant protein (serum albumin) : disaccharide 1 : 1 and 1 : 3 (w/w) freeze-dried systems for the first time. In samples with a higher disaccharide content, the protein-protein distances are longer for both populations, while the fraction of the protein population with a shorter protein-protein distance is lower. Both factors would favor better stability against aggregation for disaccharide-rich protein formulations.