Determination of nanostructure of liposomes containing two model drugs by X‐ray scattering from a synchrotron source

Small‐angle X‐ray scattering has been employed to study how the introduction of paracetamol and acetylsalicylic acid into a liposome bilayer system affects the system's nanostructure. An X‐ray scattering model, developed for multilamellar liposome systems [Pabst et al. (2000), Phys. Rev. E, 62 , 4000–4009], has been used to fit the experimental data and to extract information on how structural parameters, such as the number and thickness of the bilayers of the liposomes, thickness of the water layer in between the bilayers, size and volume of the head and tail groups, are affected by the drugs and their concentration. Even though the experimental data reveal a complicated picture of the drug–bilayer interaction, they clearly show a correlation between nanostructure, drug and concentration in some aspects. The localization of the drugs in the bilayers is discussed.     

Shallow Donors and Deep-Level Color Centers in Bulk AlN Crystals: EPR, ENDOR, ODMR and Optical Studies

The results of studies of shallow donors and deep-level color centers in bulk AlN crystals are presented. Two shallow donors (presumably oxygen located on the nitrogen site and carbon located on the aluminum site) are suggested to exhibit the DX-relaxation. Third shallow donor (presumably silicon on the Al site) shows the shallow donor behavior up to the room temperature and can be observed without light excitation at temperatures above 200 K. The values of the Bohr radius of the shallow donors are estimated. The structure of deep-level color centers (neutral nitrogen vacancy V _N) in bulk AlN crystals is determined and analyzed by electron paramagnetic resonance, electron-nuclear double resonance, optical absorption and thermoluminescence induced by X-ray irradiation. Spin-dependent recombination processes in AlN crystals are studied by means of optically detected magnetic resonance.     

Coding of Gibbs function flows from nucleotide pools

The biochemical machinery of living systems obeys kinetic laws, but is driven by Gibbs function flows. Both the kinetic and thermodynamic aspects of Gibbs gain, transmission, and utilization are considered. An information-theoretic approach is used to find conditions under which the kinetics encodes the associated Gibbs function flow with the lowest possible error.     

Stability in the Erdős–Gallai Theorem on cycles and paths,II

The Erd?s–Gallai Theorem states that for $k\ge 3$, any $n$-vertex graph with no cycle of length at least $k$ has at most $\frac{1}{2}(k?1)(n?1)$ edges. A stronger version of the Erd?s–Gallai Theorem was given by Kopylov: If $G$ is a 2-connected $n$-vertex graph with no cycle of length at least $k$, then $e\left(G\right)\le max\{h(n,k,2),h(n,k,?\frac{k?1}{2}?)\}$, where $h(n,k,a)?\left(\genfrac{}{}{0ex}{}{k?a}{2}\right)+a(n?k+a)$. Furthermore, Kopylov presented the two possible extremal graphs, one with $h(n,k,2)$ edges and one with $h(n,k,?\frac{k?1}{2}?)$ edges.In this paper, we complete a stability theorem which strengthens Kopylov’s result. In particular, we show that for $k\ge 3$ odd and all $n\ge k$, every $n$-vertex 2-connected graph $G$ with no cycle of length at least $k$ is a subgraph of one of the two extremal graphs or $e\left(G\right)\le max\{h(n,k,3),h(n,k,\frac{k?3}{2})\}$. The upper bound for $e\left(G\right)$ here is tight.