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The cation-induced spectral shifts and the stability constants revealed binding strength in the order Ca2+>Ba2+≫Li+>Na+>K+>Mg2+. Competitive experiments performed in a matrix of ions also indicated superior interaction of 6 and 7 with Ca2+.
In order to replace the huge mass of seven membrane-spanning helices in the natural receptor with a low molecular weight macrocycle, elements of much higher rigidity were implemented into the fourth generation of new adrenaline hosts, which should have a high degree of functional group preorganization and therefore lead to enhanced binding strength in the physiological solvent water.
Unusually their activities do not correlate with anion affinities, thus suggesting an upper limit for binding strength in the design of anion carriers.
Let us now consider the S/N-ratio of a particular probe at two conditions: (i) with x = 0, referring to the non-specific binding strength in the centre of the normal background distribution, XpPM,N ≈ 10 μ /Mc: R p = M c ⋅ X p P M, S / 10 μ ; and (ii) with x ≠ 0, i.e. XpPM,N x) ≈ 10 μ +x/Mc and R (x ) = M c ⋅ X p P M, S / 10 x + μ.
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This raised the question whether the binding strength in mouse, as measured by the number of ChIP tags, is indicative of binding site retention in human.
Avidity effects are well known to amplify the binding strength in solid-phase assays, but it is also possible that the two DS domains in a DDR dimer co-operate in collagen binding (see below).
Although nucleotide recognition by HTH-2 seems to be less important than that by HTH-1, it may significantly affect the binding strength in some cases.
Moreover, the reprogramming factors only bind transiently and show weak binding strength in intermediate reprogramming cells than ESCs or iPSCs, as observed in [ 15].
The former two measures can be scaled to values equivalent to the expression level of the PM according to (see also Eq. (24)), (35) L set = L set PM, S ≈ s c ⋅ L set MM, S ≈ (1 − s c − 1 ) − 1 ⋅ L set PM − MM, S, and finally transformed into the "set-averaged" binding strength in analogy with Eq. (32) (36) S set = X set PM, S = L set M c.
An antibody can recognize its antigen, and can evolve toward the immunogen to increase binding strength, in a process referred to as affinity maturation.
Our results were consistent with previous studies [49], [50], [51] which showed that the cooperativity of H-bonds facilitate to achieve strong binding strength in biomolecules.
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