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A list of all aligned fungal tRNase ZSs is provided in Additional file 4. Alignment revealed that like B. subtilis and human tRNase ZSs, fungal tRNase ZSs contain Motifs I-V and the PxKxRN, HEAT and HST loops.
Sequence alignment revealed that P. fucata α-amylase (Pfamy) shared the highest identity (91.6%) with Pinctada maxima.
Sequence alignment revealed that one specific region in PufX may be essential for PufX-induced core dimerization.
However, multiple sequence alignment revealed that PitA is expressed in four different variants in bacteria, and the structural complexity of these variants increases progressively.
The accuracy analysis of "cold" alignment revealed that present-day total stations (when choosing optimal measurement techniques) allow for the reliable estimation of the machine state and providing its efficient adjustment.
Multiple sequence alignment revealed that Cfi proteins were well conserved with the typical modular architecture and identical active sites throughout the vertebrates, which suggested the conserved function of Cfi.
Performing a peptide backbone alignment revealed that the 3D-structure of the peptide backbone was highly conserved [44].
Protein sequence alignment revealed that they are highly conserved in the predicted NAC DNA-binding domains (Fig. 1b).
Structural alignment revealed that ATRX and Rassf1c target the same "α2-α5" surface of DHBDAXX (Fig. 2H).
Sequence alignment revealed that LhSorTGA2 was featured with a basic leucine zipper (bZIP) domain and two glutamine rich acid domains (QI and QII).
Sequence alignment revealed that they belonged to STT3A and STT3B cluster respectively and the two genes most likely evolved independently since they located in the different clade on the phylogenetic tree.
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