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The side chain RMSF and standard deviation of ΔASAs give similar indications for many binding site residues, where residues used inconsistently across multiple complexes are the most likely to undergo conformational rearrangement.
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Multiple complexes were observed in an Electrophoretic Mobility Shift Assay using Hela cell nuclear extracts and a radioactive probe containing both putative sites (fig. 2A, lane 2).
The presence of multiple complexes is expected – really?
This suggests that it is likely that multiple complexes were also affected in those crypts.
We show that in ∼50% of crypts with any form of respiratory chain deficiency, decreased expression of subunits of multiple complexes is observed.
For example, if a protein on the periphery of multiple complexes is chosen as a seed, the resulting predicted complex may subsume the multiple complexes under an unrealistic big false complex that can not match with any real protein complex.
Here, we show that the assembly of multimeric OMPs is more strongly affected than that of monomeric OMPs when essential Bam complex components are limiting, suggesting that multiple Bam complexes are needed to assemble multimeric proteins.
This susceptibility of multimers to lowered quantities of Bam machines in the cell may indicate that multiple Bam complexes are needed to efficiently assemble multimeric proteins into the OM.
In cases where multiple OXPHOS complexes are affected, both bypasses in combination might be needed to restore electron flow.
This means that multiple proteins-DNA complexes are more thermodynamically stable than single protein-DNA complexes.
These data therefore suggest that multiple-sized TatA complexes are not essential for the effective transport of Tat substrates.
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Justyna Jupowicz-Kozak
CEO of Professional Science Editing for Scientists @ prosciediting.com