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The sequences nearly identical to the query protein (sequence identity > 90%) or with a low identity (sequence identity < 30%) were excluded from the input data.
The identity, sequence, and objects of representation of these stones are matters of controversy.
Despite this low amino acid identity, sequence comparison revealed a highly conserved heptapeptide motif HHxxxDG found in most bacterial WS/DGAT (or its deduced sequence) that is critical for the enzymatic activity.
Protein identity, sequence coverage, and false identification rates were evaluated by liquid chromatography-MS (LC/MS).
It is the first time that a leader sequence conserved among two distinct genera is observed (>70% identity sequence).
Phylogenetic analyses of the aprA sequences revealed two closely related (97.7% amino acid sequence identity) sequence types related to gammaproteobacterial aprA sequences.
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To confirm the protein identity, sequences were subjected to a profile search using Pfam [ 48].
UniRef90 (rel. 8.5) non-redundant (<90% identity) sequences were used to represent the protein space.
When we group the duplicated segments based on the sequence identities, sequence identities vary for each duplicated pair.
To determine the amino acid identities, sequences from the alignment were pairwise compared using DNAMAN 6.0.
The identity and sequence of fragments was confirmed by sequencing.
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CEO of Professional Science Editing for Scientists @ prosciediting.com