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Ideally, removal of this domain would leave the rest of ChlH unaffected structurally, if not functionally, and indeed the low-resolution structure of the ΔN159ChlH mutant and comparison with WT ChlH show that the N-terminal domain has been removed cleanly from the rest of the protein, leaving the rest of the structure apparently intact.
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Analysis of these previously uncharacterised ALK mutants and comparison with ALKF1174 mutants suggests that ALK mutations observed in neuroblastoma fall into three classes.
Analysis of the fluorescence response of these mutants and comparison with transport assays provides us with insights into the structure-function relationship of the CHL1 nitrate transceptor.
Many Hpo pathway targets, including direct growth regulators such as cycE, diap1, and Myc, are expressed at near-normal levels in Scrib module mutants, and comparison of Scrib module and Hpo mutant transcriptomes reveals limited overlap.
These comments center on the being more explicit about the limits of the work, its interpretation (especially regarding the mutants), and comparison to other studies, providing more information about certain analyses, and addressing some points for clarity of presentation and communication.
There are many ways to select mutations that increase the stability of proteins, including rational design, functional screening of randomly generated mutant libraries, and comparison of naturally occurring homologous proteins.
We finish by looking ahead to the prospects of uniting these three technologies to allow accurate, high-throughput screening of mutants and automated comparison of biological data with computer predictions.
However, our present finding on the different Ca2+ sensitivities of the UCP3 mutants and the comparison with the wild-type UCP3, provide important information that can explain the observed differences in the contribution of UCP3 mutants to mitochondrial uptake of Ca2+ supplied varyingly strong from different sources.
Parallel formation of AMP and aa-tRNAVal by wild-type and mutant E. coli ValRS and comparison of the Km values in the activation of noncognate amino acids with their concentration in the cell.
In the present work, we investigated the physiological role of NIR function of human AP endonuclease through site-directed mutagenesis and comparison of mutant APE1 activities in the BER and NIR pathways.
This expression system provides a powerful tool for the expression and comparison of mutant and/or phylogenetically diverse cellobiohydrolases in the industrially relevant cellulase production host H. jecorina.
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