Kinetics - Science topic

Did you fit also the half-saturation constant (Michealis-Menten constant) ?

Because, in your fitting procedure, you may impose a condition of your Hill coefficient to be between the biological limits and "play" around with the half-saturation constant in those ranges.

Thanks Akbar Ali Mohamad for your response. I have been checking for some of the above points you mentioned, still have not found any issue. However, some of the points are still to be checked thoroughly. Anyways thank you once again.

Here is the procedure look at is carefully i think it Will solved your worry

R = K[A][B]

COPASI: Biochemical System Simulator.

free download from copasi.org

Dear friend Sivasakthi Paramasivam

The s-CM5 sensor chip is commonly used for surface plasmon resonance (SPR) analysis to immobilize proteins for binding studies. The chip surface is coated with a thin layer of carboxymethylated dextran, and proteins are immobilized on the surface through covalent coupling or non-specific adsorption.

To store the protein immobilized s-CM5 sensor chip, it is recommended to use a buffer that is compatible with the immobilized protein and will not cause significant degradation or denaturation of the protein. HBS-EP buffer (10 mM HEPES pH 7.4, 150 mM NaCl, 3 mM EDTA, and 0.005% Tween-20) is a commonly used buffer for storing immobilized proteins on SPR sensor chips. This buffer helps to maintain the stability and activity of the immobilized protein over time.

For long-term storage of the protein immobilized s-CM5 sensor chip, it is recommended to store the chip in a sealed container or bag with the HBS-EP buffer at 4°C or -20°C. The storage time depends on the stability of the immobilized protein, but it is generally recommended to use the chip within a few weeks to a few months of immobilization to ensure optimal binding activity.

If you are measuring the conversion of NAD(P)H to NAD(P)+ at 340 nm, the absorbance decreases as the reaction progresses. You should perform your calculation using the absolute value (i.e. positive value) of the negative absorbance change.

Use Beer's Law to calculate the change in concentration of the analyte based on the absorbance change, where the absolute value of the absorbance decrease divided by the path length (0.6 cm) and divided by the extinction coefficient (6.22 mM^-1cm^-1), give the concentration change of the analyte in mM units.

The calculation of specific activity from this result requires knowing the volume of the sample that was measured and the concentration of protein that was present during the reaction.

specific activity = nanomolar concentration of product formed or substrate consumed divided by concentration of protein in mg/liter and divided by time of reaction.

Hello

If the difference between your experimental and calculated q_e is large, then maybe your adsorbent is not completely saturated and has not reached complete equilibrium. Moreover, it is better to do fitting of your kinetics data using non-linear forms of Pseudo-first-order and Pesudo-second-order models. The R² value can confirm the better fitting; if it is close to 1, your data is better fitted to that particular model.

Hello

I Will suggest you to perform non linear kinetic modelling.

But in case of linear the qe value is obtained after extrapolation of the highest value of qt. You can fine the real value of qe by plotting qt versus time and on that graph make the projection of the highest qt value of y-axis then you Will have your real qe value.

The study of combustion is important to optimize the design and operating parameters of a combustor. The combustion between the fuel and air involves the conversion of the chemical energy of the species to heat energy. Complete combustion is desirable to get the maximum thermal efficiency out of it. Incomplete combustion is not desirable as it emits hazardous unburnt hydrocarbon as well as CO2, NOx, etc to the environment.

It is clear that the weight of a unit of MASS is always the same at a given point in space-time. As for the VOLUME unit, the original statement is erroneous. In fact, the mass of a unit volume of a material increases slightly on heating according to Einstein's formula, but at the same time decreases much faster due to thermal expansion.

Because this situation is in the tight-binding regime, you should use the tight-binding equation for the equilibrium calculation.

fraction of enzyme with ligand bound=

[(K_d + R_t +L_t) - square root((K_d + P_t +L_t)^2 - 4R_tL_t)]/(2R_t)

where R_t is the receptor protein concentration and L_t is the ligand concentration (^2 means squared)

For example, if K_d=0.168 µM, R_t=14 µM and L_t=28 µM, the fraction of occupied receptor is 0.988.

Dear Mariana J. Do Amaral, it was an experiment I was trying to do a long time ago. Unfortunately, I had to move on to other experiments as it was taking a long time to standardize. However, the main problem I was facing was the magnesium ions in my running buffer as far as I can remember. Magnesium being a divalent cation was probably binding to the NTA chip surface, giving negative RU. I also had cobalt ion in the buffer containing the his-tagged protein. Besides, ribosomes being such a big molecule needed more standardization which I didn't pursue. However, as far as I can remember, all the above suggestions from other people help understand the crucial points one needs to follow in order to standardize the experiment which I left inbetween.

Hello Dr. Mukherjee, have you found these parameters? If yes, could you please share?

Tushar Debnath Deconvolution of a composite peak into its individual peaks plays an important role in the interpretation of many types of graphs including XRD, XPS, FTIR, and PL etc. In this video, I have discussed how to deconvolute simple combined peaks, composite peaks and how to correct missing data in a given peak with the help of deconvolution in OriginLab. In the case you want to further ask about it, please do comment on the specific video, I'll respond to it shortly. I have provided the practice files (OriginLab) here. Thanks

Thank you for sharing idea Madhukar Baburao Deshmukh

Dear Dr. Sajad Sohrabi ,

I appreciate your explanations very much and congratulate you on your nice published paper. In addition to your accurate interpretations, we have provided some additional information in the following paper:

Pseudo second order kinetic model.a complete step by step process...

Abdallah Bouguettoucha, I'm sorry but it seems you are confusing two terms: order of reaction and molecularity of reaction. The number of colliding molecules may influence the order of the reaction, but it does not have to, and very often it does not. Moreover, the order of the reaction applies mainly to homogeneous reactions for which the kinetic equation (rate law) has the form of a power monomial. Heterogeneous reactions are generally of no order except for those whose kinetic equation is a power monomial. Molecularity is not considered in the kinetic equations for homogeneous reactions. It can be included in the kinetic equations of heterogeneous reactions (the exponent in the denominator of the L-H equation).

Dear Arka,

Good afternoon!

I always try to keep in mind that C is an interstitial alloying element while Al, Co and Si are substitutional alloying elements n Fe based alloys (like steels).

That means that Al, Co and Si will "take the place" of Fe atoms in the crystals, differently than C, B and N that will be in the interstitial positions in both austenite and ferrite crystals...

In Fe alloys there are only 4 gammagenic alloying elements, as follows: Ni, Mn, C and N. These 4 chemical elements are, ALWAYS, austenite formers in Fe alloys.

Si is a strong alphagenic element. It means it is a ferrite former.

I would as well keep in mind that both Al and Si have strong affinity with oxygen, been considered deoxidant elements in Fe based alloys.

What I can guarantee to you is that Co will always shift the TTT curve to the left... But I do not agree that Al and Si will do the same.

Co is a very interesting alloying element in Fe alloys. Keep in mind that Co is neighbour of Fe in the periodic table! I would tell you that the important effect of reduction of stacking-fault energy (SFE) that Co creates in Fe based alloys may be the answer to this particular effect that Co will always shift the TTT curve to the left... But it is something that is not 100% explained yet.

Very interesting question... Thank you!

I hope to help you. If it makes sense to you, I invite you to read some of my papers...

And join our research team! You are very welcome!

André

Here is the problem. In the math above, [L] is not the total ligand concentration. It is the free ligand concentration. If [P] is near or above the K_d, and [L] is not >> [P], then the free and total ligand concentrations will be significantly different, and the mathematical relationships above will give incorrect results.

In the so-called tight-binding domain, which is the situation just described, you should calculate [PL] using the tight-binding (Morrison) equation.

F_PL = {(K_d + P_T + L_T) - square root[(K_d + P_T + L_T)² - 4P_TL_T]}/(2P_T)

where P_T andL_T are the total concentrations of P and L.

If it still matters, I’m currently using 0.1% phosphoric acid buffer and acetonitrile, 7:3 v/v

Dear Anas Abdullah

As Professor Frank T. Edelmann has mentioned, The CAS number is 123-31-9

All the best

Hi Subhash,

You are looking for an object tracker / feature matcher. Here below a few tools I remember of:

1) https://physlets.org/tracker/ -> it's manual, quick and dirty for analysing a small quantity of data.

2) https://opencv.org/ -> start writing some code, requires some learning curve but scales better with large amount of data ( see https://docs.opencv.org/trunk/dc/dc3/tutorial_py_matcher.html , https://stackoverflow.com/questions/42938149/opencv-feature-matching-multiple-objects, https://docs.opencv.org/trunk/dc/dc3/tutorial_py_matcher.html, and https://www.pyimagesearch.com/2018/07/23/simple-object-tracking-with-opencv/). If you start analysing frame by frame, at some point you will need to move a probabilistic model overlay ( http://www.cs.toronto.edu/~urtasun/courses/teaching.html).

3) http://www.mousemotorlab.org/deeplabcut -> this tool seems promising enough, but computationally heavy.

Keep it simple if you can.

Best,

Andrea

I use for fitting and analysis of kinetic data the Copasi software (free download from Copasi.org ). It's very powerful and friendly for users. It allows to put restrictions on almost all parameters. You may try. If you try, please, let me know which software is better for you.

Yes, it is perfectly possible to get a negative intercept value for the Weber-Morris intraparticle diffusion kinetic model. A negative intercept value is simply explained by the combined effects of surface reaction control and film diffusion processes.

Kindly read the following article to gain more insights towards the fundamentals of adsorption kinetics:

Tan, K.L., Hameed, B.H., 2017. Insight into the adsorption kinetics models for the removal of contaminants from aqueous solutions. Journal of the Taiwan Institute of Chemical Engineers. 74, 25-48.

The progress curve you described sounds like you have nearly complete inhibition from the start, with just enough activity remaining to see a slow linear increase. The slow linear increase could also be a background uncatalyzed rate. Sometimes, inhibitors, even covalent ones, are reversible, which results in a slow residual rate. This could be because the enzyme slowly destroys the inhibitor, or because the inhibitor dissociates from the enzyme intact.

It might be helpful if you share some images of your progress curves.

Thanks all

Sundeep Pothula Did you do that finally? If yes could you please let me know how you calculated the kinetic parameters from densitometry data?

I have the apoenzyme without the heme and the holoenzyme with the heme. I determine the total concentration based on the absorbance at 280 nm and also the concentration of the holoenzyme based on the heme absorbance at 406 nm. As only the holoenzyme contributes to the activity and this activity is in correlation with the heme concentration, I use only the concentration of the holoenzyme in the kinetic measurements.

The concentration of the holoenzyme in a reaction is 10 nM.

Dhiraj, indeed. It was my initial idea to test whether the different amount of apoenzyme influence the turnover rate of the holoenzyme. In my case, the apoenzyme do not influence the turnover rate. However, I'll try to get rid of the apoenzyme or reconstitute the apoenzyme with heme (it is not worked out yet) in future to avoid incorrect results and the misinterpretation.

Kevin de Keijzer thanks! I actually did when it came out :) :

https://twitter.com/lahti_johan/status/962971206994579456

https://twitter.com/lahti_johan/status/962971997671182336

Its a great one

You can use any band based on the chemical groups that do not show changes during any chemical reactions or physical reactions. However, majority of the IR bands are the contributions from multiple groups and, thus, tend to change the intensity by either chemical reactions or physical structural changes. Aliphatic CH stretching bands, in the region of 3000-2800 cm-1, are usually very stable as the potential energy distribution of these bands are nearly 99% pure. In the case of PU, you have relatively well isolated 2972 cm-1 band. However, PIR lacks this band. Yet, there are multiple bands between 2950 and 2850 cm-1 that appear to be relatively stable. Ideally, you should curve resolve these heavily overlapped bands (there are at least three bands, maybe 4) to be more accurate, but by measuring the height (absorbance), you can obtain quasi-quantitative comparison. Use the intensity of one of the band (the one near 2850 cm-1 might be good) and divide the absorbance of the band you want to compare to normalize the intensity then compare the normalized intensity of two different conditions, such as different reaction times.

Dear Mehdi Akbarifar

There is no translation of special practical work into English

With the help of Calibration Curve you can easily calculate the final concentration of dye (Ce) . For this you have to make the stock solution of dye at different concentration and take the absorbance of these solution with the help of spectrophotometer.

The dislocation contrary to the point defects at low temperatures is not with thermal equilibrium with thermostat (they can not arisen in consequence of thermal fluctuation). So is quantity is determined by another reasons of not thermal nature (for example in SPD processes). At high temperatures the mobility of dislocations grows and they go away from grain bulk and transit to the (grain) boundaries

Dear Akhil Patil, I'm answering this it may help others who are seeking the answer.

The total energy should be constant and the hourglass energy should be less than 5% of internal energy.

I apologize for the out-of-area answer

tq for the answer.

The following articles introduce the most correct manner for calculation of thermodynamic parameters and contain valuable explanations about this subject.

Journal of Molecular Liquids Volume 273, January 2019, Pages 425-434; Journal of Molecular Liquids Volume 280, 15 April 2019, Pages 298-300

Interesting Statement. Can you name some reverence?

The silane is not stable towards hydrolysis. We published as far as I know the first kinetic analyses of the siloxane formation with stoichiometric / controlled amount of water. We did not observe a back reaction. Siloxanes are like SiO2 stable.

For all of our investigations using siloxane layers on silicon wafer surfaces (a few hours in contact with ultrapure water) a significant amount of reversibility was not observed. The only tested way to “cut” the Si-C bond or to degrade the agent was to use strong UV-light.

It might be possible that the pretreatment of the glass surface was insufficient or that the "Agent" is degradated (UV, Bio,...), but Hydrolysis of the SiOSi bond from my opinion unlikely.

I recommend you to read this paper:

http://ijens.org/Vol_18_I_05/180505-3737-IJMME-IJENS.pdf

Best regards

Relative growth can otherwise be known as exponential growth rate. The following equation can be applied:

RGR =  (ln W2 - ln w1)/(t2 -t1) where,

ln = natural log

t1 = time one (e.g in days)

t2 = time two (e.g) in days)

W1 = size at time one

W2 = size at time two

Yes, the measured signal is heat flow (W). In an ideal case, isothermal DSC baseline is a completely flat line. Thus, its deviation/curvature is only caused by heat evolution during the curing process. If you integrate the isothermal heat flow signal and normalize it to the heat of 100% curing, you would obtain "curing degree vs. time" curve at certain temperature.

Care should be taken when choosing the temperature and initial heating ramp - at high temperatures the curing can occur during the initial heating ramp - quite fast heating rates are recommended. The curing peak can also partially overlap with signal transient (heating ramp -> isotherm).

If the temperature is too low, the curing is very slow and the heat flow signal can be lost in noise and long-term baseline drift.

Panjak,

I want to echo what others have said before. You need to decide what it is you are trying to model. An empirical model describing metal uptake rates by your mushrooms could be useful and is possible for your system. I think that a mechanistic model (one that explains the elementary steps of uptake) is not possible with your system. Metal ion capture, transport, and uptake involving large ligands is a very complicated process with many many elementary steps. I study relatively simple ligand exchange systems (2 ligand and 1 or 2 metal ions). If I want probe the mechanistic detail of one of my reaction systems, I need to repeat my experiments many dozens of times while varying reaction conditions (pH, ligand concentrations, etc.). Using living organisms, real soils, industrial effluents only complicates this process.

The answer is no. BET theory will get you nowhere. My understanding of phytoremediation of metals in soils is something like this: Plants (or in this case fungi) produce ligands that are excreted to the soil during the night, when the plants are respiring. These ligands chelate the metals (mostly divalent) so that they are water soluble. During the day (when plants pump water, the metals are taken up with the water. For mushrooms, the questions are: do they produce and excrete ligands?; when do they do this (is water ever returned to the soil?; and are these ligands similar to those excreted by plants? Regarding BET theory: yes, root surface area is an important property, but this alone does not tell you anything about the physicochemical process (complexation) or transport mechanism (water flow).

Dear Rick,

If we have a "slow - fast - slow" behavior, then for a single chemical reaction I associate with autocatalysis - which does not mean that each autocatalytic process has to ran like this. Of course in nature and not only there are a number of processes and phenomena of such and more complicated course.

Regards,

PS. Now we are discussing something different than in the question.

Very late answer, but something like this is done here:

Please avoid GOK, unless you have demonstrated that the peak shifts to lower temperatures with increasing doses. Fitting of a single TL curve with GOK usually does not lead to physically meaningful parameters.

I recommend the work by Sunta et al. on this topic: Sunta, C.M., Ayta, W.E.F., Chubaci, J.F.D. and Watanabe, S., 2005. A critical look at the kinetic models of thermoluminescence - II. Non-first order kinetics. J. Phys. D: Appl. Phys. 38, 95-102.

The criticism is also summarized in our recent manuscript that was just accepted for publication: E. G. Yukihara*, A. C. Coleman, R. H. Biswas, R. Lambert, F. Herman, G. King.“Thermoluminescence Analysis for Particle Temperature Sensing and Thermochronometry: Principles and Fundamental Challenges”. Radiat. Meas., in press(2018).

The way to get Vmax from the Michaelis plot (V versus [S]) in this situation is to use nonlinear regression to fit the data to the rate equation to obtain estimates of the kinetic parameters Km, Ki, and Vmax. This method can also be used, of course, when there is not substrate inhibition and is preferable to reciprocal plots.

Hi Muhammad,

Thanks for the question - I enjoyed it :)

The highest rate is at A=B=(A0+B0)/2

Please see the file attached with scribbles for deviation.

Regards,

Nikolay

Please look at Prof. Bala Subramaniam’s paper AIChE J. 63: 162-171, 2017 and his other related publications. There are publications by others in the area as well. Do a quick search. More detailed data available in industrial companies I am sure but not available to public at this time.

Hi

Output 'matsum' history in your ASCII(*DATABASE_ASCII_option) or binout file which will give you the kinetic and eroded kinetic energy of each part of your model. You can also plot resultant rbvelocity in ls-prepost.

History->part->resultant rigid body velocity

I understand more or less. Chemical reactions in the thin layer of lubricant oil presumably without concentration gradients in it. The simultaneous oxidation and degradation of the lubricant oil ingredients at unknown temperature. Unknown compounds included in the lubricant oil, but probably also additives that improve its quality. And in addition, you write about residuals on the cleaned surface.

You can analyze each component separately, but a lot easier, as in the first attached publication, groups of components with similar properties. This publication suggests too that the individual reactions of the component groups are the first order reactions. There is also information on the possible reaction scheme of groups of ingredients. This is a big help, but without kinetic data on the individual characteristics of your raw material you will not do much. Can you find such data in publications? - I do not know. Rather, you face tedious experimental study using methods adapted to your process conditions and an even more difficult interpretation of the test results. Good luck.

1. Calculate the protein-ligand binding free energy using free energy perturbation or linear response approximation (or its simplified version: linear interaction energy); you will need to run two sets of MD simulations: protein-ligand complex in solution and free ligand in solution.

2. Calculate Kd from the protein-ligand binding free energy (deltaG = RTlnKd).

Regardless of what standard or approach we use, as a result we obtain the value of two (k_o, E), three (k_o, E, n) or several numbers (ko, E(T₁), E(T₂) ....., n). These numbers have a limited physical meaning or they do not. Despite this, often, in my opinion, incorrectly, they are identified with the frequency factor, the energy / energies of activation and reaction order (as for single chemical reaction). Heating of various materials is a very complex process. One can distinguish: phase transitions like melting, sintering, glass transition, pasting (hydrocolloids) etc.; evaporation of water or, in general, the process of dehydration (biological or hydrated materials) and chemical decomposition processes including gasification processes. In addition, in the case of porous materials, transport effects may have an impact on the course of the process.

One of the reasonable approaches here is the deconvolution of the DTG curve and the analysis of the separate stages represented graphically by the individual peaks. Regards,

Vladimir Sir, I wanted to study it from those point of view.

Where it is not known what the reaction is, under what conditions it occures, no relible answer is possible. The rate of chemical reaction can decrease with time, it can also increase and then decrease (autocatalitic reaction). There is also no the relationship between the order of chemical reaction and the behavior observed - no conversion changes. And I will repeat, I do not know. which once - the term "reaction order" refers to a single chemical reaction.

Or maybe the answer is the most trivial, that is, total consumption of the substrate. Regards,

To calculate KH/KD for kinetic studies, first carry out the reaction with undeuterated com & then with deuterited compds. and measure the rates separately. Then take a ratio kH/kD to know whether the bond is broken in the slow or fast step of reaction.

Your question implies that pyrophosphate is also a product of the reaction. By coupling your reaction with pyrophosphatase you can generate two molecules of Pi per molecule of ATP hydrolysed. Measurement of Pi is routine.

Yurii V Geletii asked a question

Ill formulated questions require additional information. I came across with numerous cases when a questioner never responds, does not provide requested details, and seems to be not interested in getting an answer. Could such questions be considered as an attempt to raise RG score or a spam? Could the person who asks a question and not responds to answers be considered as a spammers?

thank you for answer

Could the discussion be over?

The reaction (process) order is primarily the result of an experiment - correct experiment, but also a mathematical description. The situation you write is possible. This depends on the range of the change in initial substrate concentration. This type of behavior can also be described using hyperbolic functions, eg well-known equations as M-M or Monod (the same mathematically). Then for low concentrations the reaction may be considered as first order and for large as zero order. As low and large, the value of K_m (K_s) is decisive . However, in the whole range of initial concentration change, the reaction (process) has no order (the definition of the reaction order), which is worth remembering. Regards,

"Starch" is a very broad term that includes a wide variety of related chemical structures, not only amylose and amylopectin, but minute amounts of associated lipids, proteins, and phosphates as well. Furthermore, the molecular weights and solubilities of the polysaccharide components of starch can vary quite a bit. In short, "starch" is not very well-defined in terms of molecular structure and Mw, at least not for the purposes of studying enzyme specificity. Maltopentaose represents a clearly defined substrate with a known structure and known Mw, and can yield much more useful information regarding enzyme specificity, kinetic parameters, etc. For modeling purposes, especially, having a low-Mw well-defined substrate is especially important. Larger malto-oligosaccharides can also be used, but maltopentaose is the largest that is readily available at reasonable prices. Smaller ones may not entirely fill up the binding site, so may be less useful. Maltopentaose is a good compromise.

Thank you. I will look into that.

Thanks for your answers :)

What role does "metal hydride" play in the chemical reaction? Catalyst ? Substrate ? or perheps ypu think of mixing of hot substrates? Approximate: Van't Hoff rule, more precisely: Arrhenius equation and parameter values.

Regards,

If you are saying " few reported literature," you are supposed to provide references.

In general, the answer is yes if photochemistry is a rate limiting step.

The most commonly followed method to study drug release kinetics is dialysis. This usually involves the drug loaded nanoparticle of a particular concentration dissolved in a suitable release medium and added in a dialysis bag. Buffer systems of different pH are used as reservoir solutions. Mechanical agitation for an extended period of time along with different reaction temperature are provided.

I would suggest you to refer articles specifically using your desired kind of nanoparticles and application for ideas on the reaction conditions such as pH and temperature.

In general, the use of numerical methods to solve systems of differential equations is necessary when carrying out the analytical solution is very difficult.

There are several programs where systems of differential equations (ODE) can be solved numerically, for example, the most famous one is MATLAB. In this program you can use the "ODE Solver" tool to solve ODE systems.

Assuming you talk about the reaction kinetics of transesterification of vegetable oil with methanol or ethanol, ODE15S is the best option since these equations are stiff. On the internet there is a lot of information on how to solve these systems through MATLAB or other programs, for example, the following link can be very helpful : https://www.mathworks.com/videos/solving-odes-in-matlab-7-stiffness-ode23s-ode15s-117651.html

Dear Mr. Shahid, I hope to have a good chance to prepare this compound immediately without using Fe and Bi oxides, because this compounds is not easy dissolved, so must using Fe and Bi salts to prepare the compound by hydro thermal method. Good luck.

Please, read this article:

Rodda J., Graham H.K. Classication of gait patterns in spastic hemiplegia and spastic diplegia: a basis for a management algorithm // Eur. J. Neurol. 2001. Vol. 8, Suppl. 5. P. 98-108.

Hi, 

If you want I can calculate the theoretical diameter of your molecule using DFT model.

Greetings,

Julián 

The currently deals with electron elastic, excitation, ionization, and attachment collisions but does not include electron-ion collisions or electron-electron collisions (a tough problem). And if there are 'confined' electrons, approximation for energy transfer via e-e collisions.

 The formula of normalized electron energy distribution function, where the energy distribution F in time and space and normalized by: f sqrt(E) dE = 1

Not that the Boltzmann kinetic equation for electron distribution function in a weakly ionized plasma with the external time-varying and inhomogeneous electric field

https://journals.aps.org/pre/pdf/10.1103/PhysRevE.54.6746 

The sheath_potential increasing in my case

 In Parker and Morgan code, I mean that code I use,  the energy scale: the maximum kinetic energy, sheath_potential. The maximum kinetic energy which eedf will be tracked. The electrons are allowed to have higher energies, but they will not contribute to the eedf. The sheath_potential0 (V) multiplies the matrix defined by the sheath potential file we have. if non-positive, then sheath potential file is overwritten with entire zeros. otherwise values are multiplied by sheath_potential. 

Thank you for your interest,

Tagra

There is very nice software is called GraphPad prism, you can use it for any kinetic study, this software generate a proper fit  (rate equation) for your experimental data, also you will get K, life time of reaction (taw), and t1/2. Give it a go!

Hi there,

Linearization methods are not obsolete but they present specific disadvantages (for instance LB plot uses inverted axis which make the repartition of data points uneven on the graphics and error bar size is also greatly affected by this inversion). There are a lot of free sites on the web where you may run non linear regressions with your experimental data. This one has the advantage to propose an exhaustive list of non linear fittings:

https://mycurvefit.com/.