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Many of these expansions are for predicted hydrolases, phosphatases in particular, but their substrate specificities are either unknown or the affinity of known substrates is extremely low [47].
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Also, these substrates are extremely variable and traditional techniques often do not guarantee a standardized product.
It was of particular interest that the Ag/GL-5/2.5-18 aSERSsubstratetrate gave the most intense arsenate peak among all eight Ag/GL substrates, while the peaks from Ag/GL-5/2.5-2 Ag/GL-5/2.5-2 Ag/GL-5/2.5-2es were extremely weand
The region where the difference in T95 was small had either: (1) a small k d,S, such that the difference between k d,S and 1/10 k d,C was too small to distinguish C and S and the two substrates were degraded with similar timing; or (2) a large k c, such that the degradation of both substrates was extremely fast (i.e., T95 was very small; white regions in Figs. 5a and 6a).
However, due to the complex nature of dental cavities that may present very dry or very wet regions in the same tooth, achieving optimal hydration of the substrate is extremely difficult [4].
The first motif is a common feature of many proteins and suggests that the chance of CAPN3 encountering a substrate is extremely high.
Consequently, the carrier is trapped in the low energy levels of the matrix or cytosolic state in agreement with the experimental observations that the inter-conversion between states in the absence of substrate is extremely slow [4].
Since the dislocations from the substrate are extremely much lower than the dislocation generated from other sources, the MDs are considered as the main source of TDs.
On the contrary, although, at room temperature (RT), the SERS intensity of 4-MBA on Ag@Al2O3/10 was ~70 % in comparison with that on uncoated Ag NRs, this substrate was extremely robust in SERS performance at elevated temperatures.
Unfortunately experimental data on substrate specificity is extremely difficult to obtain, and the literature information is incomplete.
The catalytic domains of all MMPs share high amino-acid similarity, and their active sites are extensively conserved, thus differentiating between MMPs with small molecule substrates or inhibitors is extremely difficult (Zarrabi et al, 2011).
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