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Multiple alignments of protein sequences were constructed by using the Muscle program [ 31], followed by a minimal manual correction on the basis of local alignments obtained using PSI-BLAST [ 30] and HHpred [ 21].
Multiple alignments of protein sequences were constructed by combining the results obtained with the PROMALS program [ 68] and the MUSCLE program [ 69], followed by a minimal manual correction on the basis of local alignments obtained using PSI-BLAST [ 66].
Multiple alignments of protein sequences were constructed by using the Promals3D program [ 39], followed by a minimal manual correction on the basis of local alignments obtained using PSI-BLAST [ 37] and HHpred [ 11].
Multiple alignments of protein sequences were constructed by using the MUSCLE program [ 63], followed by a minimal manual correction on the basis of local alignments obtained using PSI-BLAST [ 60] and HHpred [ 62].
Multiple alignments of protein sequences were constructed by using MUSCLE program [ 24], followed by a minimal manual correction on the basis of local alignments obtained using PSI-BLAST [ 9].
Multiple alignments of protein sequences were constructed by combining the results obtained with the PROMALS program [ 52] and the MUSCLE program [ 53], followed by a minimal manual correction on the basis of local alignments obtained using PSI-BLAST (see Additional File 1).
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Note that the local alignments and the score of local alignments were provided by CHAOS.
For the selected alignments, all unaligned bases in 3′ ends of local alignments were regarded as non-templated additions.
Percent identity (PID) and percentage of aligned length (PL) were calculated as measures of local alignment.
It uses the output from Clustal as well as another local alignment program LALIGN, which finds multiple regions of local alignment between two sequences.
This is equivalent to the usual definition of local alignment, i.e. the optimal global alignment of two subsequences.
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