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It is well known that the Aβ aggregation is a nucleation dependent process and that the lag phase of aggregation can be eliminated by adding preformed aggregates as 'seeds' to monomeric Aβ42 [49].
The second phase of aggregation is that of the audience.
It is worth revealing that the gain in lifetime is achieved by sending the entropy of nodes in the first phase of aggregation followed by reduced data transmission (expected value) in second phase.
Electron microscopy showed that the fibrils resulting from the second phase of aggregation were straight, cablelike, and about 13 nm wide, in contrast to the homogeneous twisted-ribbon morphology of apoC-II fibrils formed under lipid-free conditions.
Increasing the concentration of wild-type αB-crystallin prolonged the lag phase of aggregation and decreased the change in light scattering due to protein precipitation such that it was completely suppressed at a 1.0 0.4 molar ratio of insulin: αB-crystallin (data not shown).
At a 1.0 0.14 molar ratio of insulin: αB-crystallin the lag phase of aggregation was the same as when insulin was incubated alone (10 min), but the rate of aggregation was decreased such that the amount of protein precipitation after 90 min was reduced by 40±3% (Fig. 2C).
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A mathematical model correlating the operation parameters with S at different phases of aggregation was developed and experimentally proved to be able to predict S with varied operation parameters.
Here we examine the apoE Aβ interactions by measuring the effect of apoE on the different phases of aggregation of Aβ.
In the second phase, effects of aggregation (decrease in photoluminescence intensity and red shift of photoluminescence band) are seen in quantum dots solution without protein (Figure 3a).
Rather does it indicate existence of another species during the initial phase of the aggregation, in addition to monomers and fibers.
α-Synuclein granules were obtained in the middle of the lag phase of the aggregation kinetics.
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