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Briefly, this method requires to measure the fluorescence decay signal of a reference solution (ref), whose decay kinetic has been previously characterized, instead of the irf by scattered laser light.
Specifically, two NMR structures clearly show that the NLRC1 CARD forms a monomer in solution (ref (43) and PDB entry 2DBD), while two crystal structures show that the NLRC1 CARD forms disulfide-linked dimers.
After washing the plates 5 times with PBST, 100 μl of 3,3′,5,5′-tetramethylbenzidine 3,3′,5,5′-tetramethylbenzidinema) was added TMBeach well and incubated for 15 min with solution
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The higher fluorescence intensities seen for the sera compared to the serum proteins could not be attributed to their respective protein concentrations since the sera contained on average 3 to 6 times more proteins than the protein solutions (32 mg/ml for FBS and 60 mg/ml for HS vs. 10 mg/ml for each protein solution; see ref. [4]).
Before the analysis, the cells were washed twice with HEPES-buffered saline solution (HBSS; ref. 23), which also served as the incubation medium in the experiments.
The results of LAPM have been compared with exact solutions and ref. [16] for α = 1.
Similarly, such gradual transformation was observed for (BiFeO3 1 − x –(SrTiO3) x solid solutions in Ref. [44], where the structural transformation proceeded for x = 0.5 0.7 with the multiphase region in between.
In order to simulate the environment of the living organism and avoid dehydration in air, the sample is soaked in the physiological saline solution as Refs. [ 14, 31].
We will here reproduce the solutions of Refs. [12,31,45].
In addition, for Example 2, it is observed that the computational solution (x^= 0,3.3333,0)) of Ref. [4] does not satisfy the constraint (x_{1}+6x_{2}+2x_{3} leq 10), i.e., (x^) is infeasible.
In the following we shall employ, in fact, the solutions obtained in Ref. [26] as the zeroth approximation of the problem with a doped dot.
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