Kinetics of gypsum crystal growth from high ionic strength solutions: A case study of Dead Sea – seawater mixtures

The assembly kinetics of microtubule protein are altered by ionic strength, temperature and Mg2+, but not by pH. High ionic strength (I0.2), low temperature (T less than 30 degrees C) and elevated Mg2+ (greater than or equal to 1.2 mM) induce a transition from biphasic to monophasic kinetics. Comparison of the activation energy obtained for the fast biphasic step at low ionic strength (I0.069) shows excellent agreement with the values obtained at high ionic strength, low temperature and elevated Mg2+. From this observation it can be implied that the tubulin-containing reactant of the fast biphasic event is also the species that elongates microtubules during monophasic assembly. Second-order rate constants for biphasic assembly are 3.82(+/- 0.72) x 10(7) M-1.s-1 and 5.19(+/- 1.25) x 10(6) M-1.s-1, and for monophasic assembly the rate constant is 2.12(+/- 0.56) x 10(7) M-1.s-1. The microtubule number concentration is constant during elongation of microtubules for biphasic and monophasic assembly.

Download Full-text

Probing the charge of reactive sites at the mineral-water interface: Effect of ionic strength on crystal growth kinetics of fluorite

Geochimica et Cosmochimica Acta ◽

10.1016/s0016-7037(97)00032-x ◽

1997 ◽

Vol 61 (9) ◽

pp. 1871-1877 ◽

Cited By ~ 5

Author(s):

Victoria L. Knowles-Van Cappellen ◽

Philippe Van Cappellen ◽

Christine L. Tiller

Keyword(s):

Crystal Growth ◽

Ionic Strength ◽

Growth Kinetics ◽

Mineral Water ◽

Interface Effect ◽

Water Interface ◽

Crystal Growth Kinetics ◽

Kinetics Of

Download Full-text

Kinetics of Cyanate Decomposition in Alkaline Solutions of High Ionic Strength: The Catalytic Effect of Bicarbonate

Industrial & Engineering Chemistry Research ◽

10.1021/ie034189+ ◽

2004 ◽

Vol 43 (16) ◽

pp. 4815-4821 ◽

Cited By ~ 1

Author(s):

Nikolai DeMartini ◽

Dmitry Yu. Murzin ◽

Mikael Forssén ◽

Mikko Hupa

Keyword(s):

Ionic Strength ◽

Catalytic Effect ◽

High Ionic Strength ◽

Alkaline Solutions ◽

Kinetics Of

Download Full-text

The effect of a phosphonate-based antiscalant on the morphology and precipitation kinetics of gypsum: The Red Sea – Dead Sea project

E3S Web of Conferences ◽

10.1051/e3sconf/20199804011 ◽

2019 ◽

Vol 98 ◽

pp. 04011

Author(s):

Amit G Reiss ◽

Jiwchar Ganor ◽

Ittai Gavrieli

Keyword(s):

Crystal Growth ◽

Surface Water ◽

Red Sea ◽

Induction Time ◽

Entire Range ◽

Dead Sea ◽

Precipitation Kinetics ◽

Batch Experiments ◽

Gypsum Precipitation ◽

Kinetics Of

The proposed plan for the 'Red Sea – Dead Sea project' has raised concerns that the surface water of the Dead Sea would turn white due to gypsum precipitation. The occurrence of such an event would depend on the precipitation kinetics and the morphology of the precipitating crystals. Batch experiments were conducted to study the effect of a phosphonate-based antiscalant on the precipitation kinetics and morphology of gypsum under the conditions of this project. Addition of the antiscalant was found to increase the induction time by a factor of 1.2-5 over the entire range of Dead Sea – Seawater mixtures investigated, depending on brine composition. Once nucleation occurred, the antiscalant also slowed the crystal growth by a factor of 1.2-3. However, when the solutions were seeded with gypsum, the rate of crystal growth with and without antiscalant were similar, within uncertainty. More crystals precipitated from unseeded solutions with no antiscalant and the crystals were smaller and less tabular than those precipitated from unseeded solutions with antiscalant.

Download Full-text

Temperature-dependent growth of protein crystals with temperature-independent solubility: case study of apoferritin

CrystEngComm ◽

10.1039/d0ce00654h ◽

2020 ◽

Vol 22 (26) ◽

pp. 4478-4488

Author(s):

Ivaylo L. Dimitrov

Keyword(s):

Crystal Growth ◽

Growth Kinetics ◽

Growth Analysis ◽

Small Variation ◽

Protein Crystals ◽

Temperature Dependent ◽

Dependent Growth ◽

Kinetics Of

Combined diffusion- and interface-controlled crystal growth analysis elucidates the temperature-dependent growth kinetics of protein crystals at a relatively small variation of supersaturation.

Download Full-text