Simple analytical approximation for rotationally inelastic rate constants based on the energy corrected sudden scaling law

1981 ◽  
Vol 74 (7) ◽  
pp. 3939-3946 ◽  
Author(s):  
Neil Smith ◽  
David E. Pritchard
1990 ◽  
Vol 142 (1) ◽  
pp. 25-33 ◽  
Author(s):  
I.K. Dmitrieva ◽  
S.K. Pogrebnya ◽  
P.I. Porshnev

2021 ◽  
Vol 2021 ◽  
pp. 1-8
Author(s):  
Junyi He ◽  
Junnan Zhang ◽  
Cheng Song ◽  
Mengxiang Wu

In this study, we consider a multiway massive multi-input multi-output (MIMO) relay network over Rician fading channels, where all users intend to share their information with the other users via amplify-and-forward (AF) relays equipped with a great number of antennas. More practical, the imperfect channel state information (CSI) is taken into account. To evaluate the performance of the considered networks, we derived an analytical approximation expression for the spectral efficiency with zero-forcing (ZF) receivers in a closed form. To obtain more insights, the asymptotic analysis as the number of relay antenna approaching infinity is carried out. Finally, the power scaling law is analyzed for two scenarios. The results reveal that (1) massive MIMO is capable of compensating the loss caused by Rician fading, (2) the sum spectral efficiency increases with the increase of the Rician factor, and (3) deploying large-scale antenna is effective to save cost and keep performance.


1988 ◽  
Vol 60 (02) ◽  
pp. 247-250 ◽  
Author(s):  
H R Lijnen ◽  
L Nelles ◽  
B Van Hoef ◽  
F De Cock ◽  
D Collen

SummaryRecombinant chimaeric molecules between tissue-type plasminogen activator (t-PA) and single chain urokinase-type plasminogen activator (scu-PA) or two chain urokinase-type plasminogen activator (tcu-PA) have intact enzymatic properties of scu-PA or tcu-PA towards natural and synthetic substrates (Nelles et al., J Biol Chem 1987; 262: 10855-10862). In the present study, we have compared the reactivity with inhibitors of both the single chain and two chain variants of recombinant u-PA and two recombinant chimaeric molecules between t-PA and scu-PA (t-PA/u-PA-s: amino acids 1-263 of t-PA and 144-411 of u-PA; t-PA/u-PA-e: amino acids 1-274 of t-PA and 138-411 of u-PA). Incubation with human plasma in the absence of a fibrin clot for 3 h at 37° C at equipotent concentrations (50% clot lysis in 2 h), resulted in significant fibrinogen breakdown (to about 40% of the normal value) for all two chain molecules, but not for their single chain counterparts. Preincubation of the plasminogen activators with plasma for 3 h at 37° C, resulted in complete inhibition of the fibrinolytic potency of the two chain molecules but did not alter the potency of the single chain molecules. Inhibition of the two chain molecules occurred with a t½ of approximately 45 min. The two chain variants were inhibited by the synthetic urokinase inhibitor Glu-Gly-Arg-CH2CCl with apparent second-order rate constants of 8,000-10,000 M−1s−1, by purified α2-antiplasmin with second-order rate constants of about 300 M−1s−1, and by plasminogen activator inhibitor-1 (PAI-1) with second-order rate constants of approximately 2 × 107 M−1s−1.It is concluded that the reactivity of single chain and two chain forms of t-PA/u-PA chimaers with inhibitors is very similar to that of the single and two chain forms of intact u-PA.


1977 ◽  
Vol 38 (03) ◽  
pp. 0677-0684 ◽  
Author(s):  
Raymund Machovich ◽  
Péter Arányi

SummaryHeat inactivation of thrombin at 54° C followed first order kinetics with a rate constant of 1.0 min−1 approximately. Addition of heparin resulted in protection against thermal denaturation and, at the same time, rendered denaturation kinetics more complex. Analysis of the biphasic curve of heat inactivation in the presence of heparin revealed that the rate constants of the second phase changed systematically with heparin concentrations. Namely, at 4.5 × 10−6M, 9 × 10−6M, 1.8 × 10−5M and 3.6 × 10−5M heparin concentrations, the rate constants were 0.27 min−1, 0.17 min−1, 0.11 min−1 and 0.06 min−1, respectively.Sulfate as well as phosphate ions displayed also enzyme protection against heat inactivation, however, the same effect was obtained already at a heparin concentration, lower by three orders of magnitude.The kinetics of enzyme denaturation was not affected by calcium ions, whereas in the presence of heparin the inactivation rate of thrombin changed, i. e. calcium ions abolished the biphasic character of time course of thermal denaturation.Thus, the data suggest that calcium ions contribute to the effect of heparin on thrombin.


2017 ◽  
Vol 137 (4) ◽  
pp. 326-333
Author(s):  
Chiaki Nagai ◽  
Kenji Inukai ◽  
Masato Kobayashi ◽  
Tatsuya Tanaka ◽  
Kensho Abumi ◽  
...  

2012 ◽  
Vol 40 (2) ◽  
pp. 124-150
Author(s):  
Klaus Wiese ◽  
Thiemo M. Kessel ◽  
Reinhard Mundl ◽  
Burkhard Wies

ABSTRACT The presented investigation is motivated by the need for performance improvement in winter tires, based on the idea of innovative “functional” surfaces. Current tread design features focus on macroscopic length scales. The potential of microscopic surface effects for friction on wintery roads has not been considered extensively yet. We limit our considerations to length scales for which rubber is rough, in contrast to a perfectly smooth ice surface. Therefore we assume that the only source of frictional forces is the viscosity of a sheared intermediate thin liquid layer of melted ice. Rubber hysteresis and adhesion effects are considered to be negligible. The height of the liquid layer is driven by an equilibrium between the heat built up by viscous friction, energy consumption for phase transition between ice and water, and heat flow into the cold underlying ice. In addition, the microscopic “squeeze-out” phenomena of melted water resulting from rubber asperities are also taken into consideration. The size and microscopic real contact area of these asperities are derived from roughness parameters of the free rubber surface using Greenwood-Williamson contact theory and compared with the measured real contact area. The derived one-dimensional differential equation for the height of an averaged liquid layer is solved for stationary sliding by a piecewise analytical approximation. The frictional shear forces are deduced and integrated over the whole macroscopic contact area to result in a global coefficient of friction. The boundary condition at the leading edge of the contact area is prescribed by the height of a “quasi-liquid layer,” which already exists on the “free” ice surface. It turns out that this approach meets the measured coefficient of friction in the laboratory. More precisely, the calculated dependencies of the friction coefficient on ice temperature, sliding speed, and contact pressure are confirmed by measurements of a simple rubber block sample on artificial ice in the laboratory.


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