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Partial protein trypsin digestions can be evaluated based on multiple peptide to protein alignment information presented in the database.
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The information presented in this Database includes a list of published three-dimensional structures for histones and histone fold-containing proteins, as well as manually curated multiple sequence alignments for each histone family.
The detailed alignment information is presented in Additional file 2: Table S1, including total numbers of reads, mapped reads, and unique mapped reads.
A more comprehensive alignment is presented in the Supplementary Information and Guillemin et al. To obtain soluble stable recombinant human Bcl-B (Uniprot: Q9HD36) protein from E. coli fermentations for our structural studies, we mutated the cysteines 20 and 128 to serine and deleted 27 C-terminal residues in the predicted TM region.
Bisulphite primer information is presented in Supplementary information, Table S5.
Primer information is presented in Supplementary information, Table S5.
We evaluated both the pairwise registration and the complete multi-view alignment pipeline presented in Section "Pairwise alignment technique'' and SectionMulti-view alignment pipeline, respectively through a series of tests performed on the datasets presented in Section "Acquired datasets".
A SEM image of this edge-driven preferential alignment is presented in Figure 4.
Alignment is presented in Figure S1 and available upon request.
We chose this method because of its robustness and its ability to take advantage of information present in the form of insertion/deletion events in the alignment.
In contrast to conventional methods, the signature method utilizes information present in the sequences that may not be analyzable with conventional alignments, such as additional sequences at the beginning or the end of alignments.
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