Structure of HEPES-Reduced δ‑MnO2 Nanosheets.

Sorption of Metal Ions on Clay Minerals: II. Mechanism of Co Sorption on Hectorite at High and Low Ionic Strength and Impact on the Sorbent Stability

Recent atomic 3-D reconstructions of the acto-myosin interface suggest that electrostatic interactions are important in the initial phase of cross-bridge formation. Earlier biochemical studies had also given strong evidence for the ionic strength dependence of this step in the cross-bridge cycle. We have probed these interactions by altering the ionic strength (Gamma/2) of the medium mainly with K+, imidazole+ and EGTA2- to vary charge shielding. We examined the effect of ionic strength on the kinetics of rigor development at low Ca2+ (experimental temperature 18-22 degrees C) in chemically skinned single fast-twitch fibres of mouse extensor digitorum longus (EDL) muscle. On average the delay before rigor onset was 10 times longer, the maximum rate of rigor tension development was 10 times slower, the steady-state rigor tension was 3 times lower and the in-phase stiffness was 2 times lower at high (230 mM) compared to low (60 mM) ionic strength. These results were modelled by calculating ATP depletion in the fibre due to diffusional loss of ATP and acto-myosin Mg.ATPase activity. The difference in delay before rigor onset at low and high ionic strength could be explained in our model by assuming a 15 times higher Mg.ATPase activity and a threefold increase in Km in relaxing conditions at low ionic strength. Activation by Ca2+ induced at different time points before and during onset of rigor confirmed the calculated time course of ATP depletion. We have also investigated ionic strength effects on rigor development with the activated troponin/tropomyosin complex. ATP withdrawal at maximum activation by Ca2+ induced force transients which led into a "high rigor" state. The peak forces of these force transients were very similar at low and high ionic strength. The subsequent decrease in tension was only 10% slower and steady-state "high rigor" tension was reduced by only 27% at high compared to low ionic strength. Addition of 10 mM phosphate to lower cross-bridge attachment strongly suppressed the transient increases in force at high ionic strength and reduced the steady-state rigor tension by 17%. A qualitatively similar but smaller effect of phosphate was observed at low ionic strength where steady-state rigor force was reduced by 10%. The data presented in this study show a very strong effect of ionic strength on rigor development in relaxed fibres whereas the ionic strength dependence of rigor development after thin filament activation was much less. The data confirm the importance of electrostatic interactions in cross-bridge attachment and cross-bridge-attachment-induced activation of thin filaments.

Foam Fractionation of Binary Mixtures of Lysozyme and Albumin

The viscosity of histone‐depleted nucleohistone has been measured at high and low ionic strength. Native nucleohistone at low ionic strength and f1‐depleted nucleohistone at both low and high ionic strength all have the same intrinsic viscosity of 10.0 dl/g. This implies that these molecules are not flexible but behave in solution as rigid particles. On the assumption that they are rods they have a weight‐average length of 1160 ± 120 nm and diameter 5.6 ± 0.3 nm. The DNA is compressed in the rod to give an increase in mass per unit length for the DNA of 5.0 ± 0.5.By contrast the intrinsic viscosity of nucleohistone depleted of f1, f2a2 and 75% of F2b and F3, varies with ionic strength in the manner typical of a flexible polyelectrolyte. The shapes of the sedimentation boundaries measured at high ionic strength of depleted nucleohistone show that the dissociation of histone from DNA takes place so that all molecules are depleted to the same extent. It thus has a conformation intermediate between that of native nucleohistone and DNA.Polyacrylamide gel electrophoresis of histones removed by 1.0 M NaCl using a technique capable of resolving all five main histone fractions, shows that if one fraction only is responsible for supercoiling nucleohistone it must be f2a2.

Zinc isotope fractionation during adsorption to calcite at high and low ionic strength

Transport and deposition of microplastic particles in saturated porous media: Co-effects of clay particles and natural organic matter

Self-assembly of misfolded proteins into ordered fibrillar structures is a fundamental property of a wide range of proteins and peptides. This property is also linked with the development of various neurodegenerative diseases such as Alzheimer’s and Parkinson’s. Environmental conditions modulate the misfolding and aggregation processes. We used a peptide, CGNNQQNY, from yeast prion protein Sup35, as a model system to address effects of environmental conditions on aggregate formation. The GNNQQNY peptide self-assembles in fibrils with structural features that are similar to amyloidogenic proteins. Atomic force microscopy (AFM) and thioflavin T (ThT) fluorescence assay were employed to follow the aggregation process at various pHs and ionic strengths. We also used single molecule AFM force spectroscopy to probe interactions between the peptides under various conditions. The ThT fluorescence data showed that the peptide aggregates fast at pH values approaching the peptide isoelectric point (pI = 5.3) and the kinetics is 10 times slower at acidic pH (pH 2.0), suggesting that electrostatic interactions contribute to the peptide self-assembly into aggregates. This hypothesis was tested by experiments performed at low (11 mM) and high (150 mM) ionic strengths. Indeed, the aggregation lag time measured at pH 2 at low ionic strength (11 mM) is 195 h, whereas the lag time decreases ∼5 times when the ionic strength is increased to 150 mM. At conditions close to the pI value, pH 5.6, the aggregation lag time is 12 ± 6 h under low ionic strength, and there is minimal change to the lag time at 150 mM NaCl. The ionic strength also influences the morphology of aggregates visualized with AFM. In pH 2.0 and at high ionic strength, the aggregates are twofold taller than those formed at low ionic strength. In parallel, AFM force spectroscopy studies revealed minimal contribution of electrostatics to dissociation of transient peptide dimers.

Transport behavior of variable charge soil particle size fractions and their influence on cadmium transport in saturated porous media

ABSTRACTNine combinations of sodium chloride (NaCl), potassium chloride (KCI), and magnesium chloride (MgCl2,) at high and low ionic strengths (IS) (0.42 and 0.21 respectively) and low IS with 0.13% tripotassium phosphate (K3PO4) were used to determine the effects of a reduction or partial replacement of sodium on bologna characteristics and acceptability. The NaCl‐MgCl2 had significantly (P < 0.05) less stable and firm emulsion and compression hardness than NaCl or NaCl‐KCl treatments. Low IS treatments had significantly less stable and firm emulsions and lower compression hardness than high IS treatments. Adding PO4 to low IS treatments produced products similar to high IS treatments. Only slight textural changes occurred in products after 14 days of cooler (1°C) storage. High IS NaCl and NaCl‐KCl and low IS NaCl‐PO4, NaCl‐MgCl2 ‐PO4 and NaCl‐KCl‐PO4 were found acceptable for flavor, texture, and color by consumer panels.

The electrophoretic distribution of RNA synthesized in vitro by isolated rat liver nuclei

By competition hybridization experiments it is shown, that RNA synthesized in vitro by RNA polymerase on T4‐DNA at high ionic strength, like that synthesized at low ionic strength, contains only early RNA species. However, the product obtained at high ionic strength contains sequences not synthesized at low ionic strength. This is attributed to the early arrest of synthesis at low ionic strength.

Previous studies on the self-assembly of capsid protein CA of human immunodeficiency virus type 1 (HIV-1) in vitro have provided important insights on the structure and assembly of the mature HIV-1 capsid. However, CA polymerization in vitro was previously observed to occur only at very high ionic strength. Here, we have analyzed the effects on CA assembly in vitro of adding unrelated, inert macromolecules (crowding agents), aimed at mimicking the crowded (very high macromolecular effective concentration) environment within the HIV-1 virion. Crowding agents induced fast and efficient polymerization of CA even at low (close to physiological) ionic strength. The hollow cylinders thus assembled were indistinguishable in shape and dimensions from those formed in dilute protein solutions at high ionic strength. However, two important differences were noted: (i) disassembly by dilution of the capsid-like particles was undetectable at very high ionic strength, but occurred rapidly at low ionic strength in the presence of a crowding agent, and (ii) a variant CA from a presumed infectious HIV-1 with mutations at the CA dimerization interface was unable to assemble at any ionic strength in the absence of a crowding agent; in contrast, this mutation allowed efficient assembly, even at low ionic strength, when a crowding agent was used. The use of a low ionic strength and inert macromolecules to mimic the crowded environment inside the HIV-1 virion may lead to a better in vitro evaluation of the effects of conditions, mutations or/and other molecules, including potential antiviral compounds, on HIV-1 capsid assembly, stability and disassembly.

Adsorption of the High Molecular Weight Glutenin Subunit 1Dx5 Compared to the 58-kDa Central Repetitive Domain and α-gliadins

This study aimed to investigate the diffusivities of lysozyme (LYS), ovalbumin (OVA), and hyaluronic acid (HA) in buffered solvents using dynamic light scattering (DLS). For protein/solvent and HA/solvent binary systems, the diffusion coefficients of protein or HA were obtained from autocorrelation function (ACF) curve fitting. Whereas, for protein/HA/solvent ternary systems, the two eigenvalues of the mutual diffusion coefficient matrix were obtained from ACF curve fitting. The results of binary systems showed that at low ionic strength, the diffusion coefficients of protein and HA increased linearly with concentration; at high ionic strength, the diffusion coefficients of OVA and LYS were independent on protein concentration; for HA, the positive linear relationship between diffusion coefficient and concentration existed at high and low ionic strengths, but the slope at high ionic strength was smaller compared to that at low ionic strength. For OVA/HA/solvent ternary systems, the sum of two eigenvalues (D1DLS + D2DLS) was slightly smaller compared to (DOVA + DHA), where DOVA and DHA were the diffusion coefficients in their binary systems. On the contrary, for LYS/HA/solvent ternary systems, (D1DLS + D2DLS) were significantly smaller than (DLYS + DHA) and the diffusion coefficients in binary and ternary systems exhibited an opposite trend with respect to ionic strength change. The DLS and MD simulation results indicated strong attractive intermolecular interaction existed between LYS and HA molecules, especially at low ionic strength. By using DLS, it was possible to characterize the diffusion coefficients of diluted protein/HA binary and ternary systems.

This study investigated the influence of carbon nanotubes (CNTs) on the transport and retention behaviors of bacteria (E. coli) in packed porous media at both low and high ionic strength in NaCl and CaCl2 solutions. At low ionic strengths (5 mM NaCl and 0.3 mM CaCl2), both breakthrough curves and retained profiles of bacteria with CNTs (both 5 and 10 mg L(-1)) were equivalent to those without CNTs, indicating the presence of CNTs did not affect the transport and retention of E. coli at low ionic strengths. The results were supported by those from cell characterization tests (i.e., viability, surface properties, sizes), which showed no significant difference between with and without CNTs. In contrast, breakthrough curves of bacteria with CNTs were lower than those without CNTs at high ionic strengths (25 mM NaCl and 1.2 mM CaCl2), suggesting that the presence of CNTs decreased cell transport at high ionic strengths. The enhanced bacterial deposition in the presence of CNTs was mainly observed at segments near the column inlet, leading to much steeper retained profiles relative to those without CNTs. Additional transport experiments conducted with sand columns predeposited with CNTs revealed that the codeposition of bacteria with CNTs, as well as the deposition of the cell-CNTs cluster formed in cell suspension due to cell bridging effect, largely contributed to the increased deposition of bacteria at high ionic strengths in porous media.