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Water condensation condition under dynamic

Figure 3. Water Condensation Condition in the Gel under Dynamic Temperature Change. Figure 3. Water Condensation Condition in the Gel under Dynamic Temperature Change.
A triple point is a point where three phase boundaries meet. For water, it occurs at 4.6 Torr and 0.01°C (see Fig. 8.5). At the triple point, all three phases (ice, liquid, and vapor) coexist in dynamic equilibrium. Under these conditions, water molecules leave ice to become liquid and return to form ice at the same rate liquid vaporizes and vapor condenses at the same rate and ice sublimes and vapor condenses directly to ice again at the same rate. The location of the triple point of a substance is a fixed property of that substance and cannot be changed by changing the conditions. The triple point of water is used to define the size of the kelvin by definition, there are exactly 273.16 kelvins between absolute zero and the triple point of water. The normal freezing point of water is found to lie 0.01 K below the triple point, so 0°C corresponds to 273.15 K. [Pg.502]

As an example of a membrane model, phospholipid monolayers with negative charge of different density were used. It had already been found ( ) and discussed O) that the physical and biological behavior of phospholipid monolayers at air-water interfaces and of suspensions of liposomes are comparable if the monolayer is in a condensed state. Two complementary methods of surface measurements (using radioactivity and electrochemical measurements), were used to investigate the adsorption and the dynamic properties of the adsorbed prothrombin on the phospholipid monolayers. Two different interfaces, air-water and mercury-water, were examined. In this review, the behavior of prothrombin at these interfaces, in the presence of phospholipid monolayers, is presented as compared with its behavior in the absence of phospholipids. An excess of lipid of different compositions of phos-phatidylserine (PS) and phosphatidylcholine (PC) was spread over an aqueous phase so as to form a condensed monolayer, then the proteins were inject underneath the monolayer in the presence or in the absence of Ca. The adsorption occurs in situ and under static conditions. The excess of lipid ensured a fully compressed monolayer in equilibrium with the collapsed excess lipid layers. The contribution of this excess of lipid to protein adsorption was negligible and there was no effect at all on the electrode measurements. [Pg.104]

Nitromethane decomposes under pressure when heated to temperatures above 440K at pressures greater than 1.6 GPa. Both pressure and temperature accelerate the rate of decomposition. The condensed product residues are mainly ammonium formate and water in addition to nonretrievable volatile gases. More than one reaction mechanism appears to be present as indicated by the complex kinetic results. A proposed bimolecular decomposition mechanism is presented that can account for the observed positive pressure dependence of the reaction rate and the experimentally detected reaction products. Nitromethane undergoes a catastrophic reaction under certain dynamic stress conditions in the DAG at room temperature. The sensitivity level to the initiation of this reaction appears to be crystal orientation dependent with respect to the applied stress in the DAC. The resulting opaque solid residue is amorphous and carbonaceous and stable to temperatures in excess of 573 K. Deuterated nitromethane was not observed to undergo this catastrophic reaction. [Pg.409]


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