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In our previous study, we determined Kd,n to be 16 μM for Egr-1 under the identical buffer conditions with 150 mM KCl.
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CD experiments were performed to determine the helical content of the human centrins under identical buffer conditions.
Narrowing of the W291 ε-HN line width in HscA386 in the presence of the linker peptide (16.7 Hz; 20.4 Hz in apo-HscA386 under identical buffer conditions) further confirms the specificity and WT-like binding interactions in the trans configuration.
Steady-state kinetics for H3 and the H3/H4 tetramer were performed under identical buffer conditions (100 mM ammonium bicarbonate and 50 mM HEPES buffer (pH 7.8) at 37 °C.
In-line probing experiments observed a 140-fold difference in KD between the Thi1 and thiM TPP aptamers under identical buffer conditions with 20 mM MgCl2.
Nevertheless, identical cis and trans-linker-induced chemical shift perturbations and a decrease in the H LWHH of ε-HN of W291 (20.4 Hz in apo-HscA386 vs 16.7 Hz in linker peptide-bound HscA386 under identical buffer conditions) are apparent, suggesting that the observed binding between the NBD and synthetic linker peptide does not emerge from nonspecific interactions.
To confirm this, we superimposed the 2D H N HSQC spectra of the untagged and GB1-tagged N-labeled ASC PYD (acquired under identical buffer conditions).
In order to determine at what concentration protein aggregation is induced by the varying salt solution conditions, the protein hydrodynamic radius was tracked using DLS measured particle size under identical buffer conditions (although not all conditions were replicated as at some of the higher ionic strengths aggregation proceeded too rapidly to accurately measure using DLS).
Nearly stoichiometric enzyme reaction mixtures were prepared under identical buffer conditions with 2.5 μM 2CNA-GPP 6 or 2AA-GPP 5, 0.1 mM IPP, and 1.7 μM UPPS of each type in a total volume of 200 μL.
The cross-linked species was eluted from the column using an identical buffer containing 2 mM d-biotin.
Meanwhile, the intensity of ZnO (002) peak for sample B was much stronger than that of ZnO (100) peak for sample A. Considering that the ZnO films were deposited and tested under the identical conditions, it demonstrated that the AlN buffer layer forced ZnO films to grow along the c-axis.
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