PubMed · 6361239
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J A Stackhouse. 1983. Voids in a mixed elastomeric impression material.. https://doi.org/10.1016/0022-3913(83)90086-0
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Hydrophobically modified dextrans, benzoyl dextran and valeryl dextran, have been used to study the interactions between tryptophan residues and benzoyl or valeryl groups by partitioning of tryptophan, tryptophan-tryptophan, (tryptophan)3, poly(lysine, tryptophan), beta-galactosidase and lysozyme in polymer aqueous two-phase systems. The two-phase systems used were polyethylene glycol (PEG)-benzoyl dextran, PEG-valeryl dextran, dextran-benzoyl dextran and dextran-valeryl dextran. Interaction between tryptophan residues and benzoyl or valeryl groups was observed by partitioning of tryptophan containing compounds to the phase containing hydrophobically modified dextran. At a certain phase composition the interactions were increased with increasing number of tryptophan per molecule. In a PEG-dextran system the partitioning of tryptophan peptides to the PEG phase was increased with increased number of tryptophan. In a PEG-benzoyl dextran system the opposite effect was obtained. At similar conditions benzoyl groups showed stronger interactions with tryptophans compared to valeryl groups. The partition coefficient of salts (sodium phosphate, NaCl, Nal and NaClO4) was determined in PEG-benzoyl dextran and PEG-valeryl dextran aqueous two-phase systems. The effect of addition of these salts on partitioning of poly(lysine, tryptophan), beta-galactosidase and lysozyme was studied. Salt effects on partitioning could be explained by the relative affinities of the ions for the polymers in the system. Charged molecules containing tryptophan were to an increasing degree partitioned to the phase for which the counterions had highest affinity. Strong effects on the partitioning of positively charged poly(lysine, tryptophan) and lysozyme were obtained with the ions I- and ClO4-.
Excitable media, which range from autocatalytic chemical systems to biological cells and tissues, can maintain organized structures in the form of rotating spiral waves of excitation. The dynamics of spiral waves in two-dimensional systems have been shown to be susceptible to control by external fields (such as electric, thermal and optical). In three dimensions, the analogues of spiral waves are scroll waves. Here we show that an external field--a temperature gradient--can be used to control a particular class of scroll waves called scroll rings. The gradient allows scroll rings to be precisely oriented in space, and their spontaneous shrinkage to be accelerated, decelerated or even reversed (so that the ring expands). The temperature gradient also influences the lifetimes of the scroll rings. We suggest that these dynamics are likely to be generic to other types of field gradients and other excitable media.
The understanding of the structural and thermodynamic properties of moderately or highly concentrated solutions is fundamental, e.g., in medicine and biology and also in many technical processes. In this work, we have used the small-angle neutron scattering method (SANS), in combination with Monte Carlo simulation, to study salt-free solutions of human serum albumin (HSA) in the concentration range up to 0.26 g ml-1. The model calculations of the theoretical SANS intensities are quite general, thus avoiding the approximation that the relative positions and orientations of the particles are independent of each other. The computation of the theoretical intensities also includes the calculation of a "thermodynamic' intensity scattered at zero angle, which is obtained via the nonideal part of the chemical potential. The latter quantity is obtained by applying the test particle method during the Monte Carlo simulations. It is found that the SANS data can be explained by a model where the HSA molecules behave as hard ellipsoids of revolution with semiaxes a = 6.8 nm, b = c = 1.9 nm. In addition to the hard core interaction, the particles are also surrounded by a soft, repulsive rectangular-shaped potential which is spherically oriented around the particles. The combination of SANS and statistical thermodynamics also allows a determination of the nonideal part of the chemical potential and the activity coefficient of HSA. As expected the activity coefficient deviates strongly from the value one (several powers of ten) already at fairly low concentrations: the effects are comparable to, or even larger than, for instance hydrophobic or van der Waals interaction.