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While in the presence of the target DNA, the probe conformation was changed and a double-stranded DNA (dsDNA) molecule was formed through the hybridization.
It may be because the columnar content and then defects decreased when the cis-cisoid conformation was changed to cis-transoid conformation.
Although the partially d-lysine substitution could improve the stability of polybia-MPI toward the tested protease, the secondary conformation was changed after modification and its antimicrobial activity decreased greatly.
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In addition to the Y116, which is the largest perturbation found in NMR, the Y112 conformation is changed significantly with and without the presence of kinase domain.
When those TFBSs' sequences are mutated and their fold conformations are changed.
Furthermore, UV Vis absorption spectroscopy and synchronous fluorescence spectra indicated that the conformation of BSA was changed.
Furthermore, synchronous fluorescence spectra and circular dichroism (CD) spectra indicated that the conformation of BSA was changed.
The results show that the conformation of BSA was changed dramatically in the presence of Er Porp by binding to the Trp residues of BSA.
The results of three-dimensional fluorescence spectra, UV vis absorption difference spectra and circular dichroism of BSA in the presence of berbamine showed that the conformation of BSA was changed.
The three dimensional fluorescence showed that the conformation of HSA was changed after its complexation with DMCTC, and the alternations of protein secondary structure were quantitatively calculated from FT-IR with reduction of α-helices content about 4.8%, β-sheet from 30.3% to 21.6% and with increases of β-turn from 15.6% to 22.2%.
This indicates that the conformation of Rad52 was changed by the binding of the ssDNA−pRPA complex, and/or the affinity of Rad52 for ssDNA is increased by interaction with the ssDNA−pRPA complex.
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CEO of Professional Science Editing for Scientists @ prosciediting.com