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In this post genomic era, when the amount of genome sequence data increases so rapidly, the high efficiency and novelty of the proposed method make it feasible for large scale classifications of microorganisms and phylogenetic studies of species with similar metabolic properties or incomplete genome sequences.
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However, this has not yet been quantified for large-scale classification of many cover types with subtle differences in complex, noisy hyperspectral patterns.
This high speed makes the proposed method well applicable to perform large-scale classification of microorganisms.
These include the following: large-scale classification, taxonomic placement of newly-sequenced genomes, and high resolution of CVTree at the rank species and below.
Both our model itself and the solving algorithm can guarantee that it can deal with large-scale classification problems with a huge number of instances as well as features.
Large-scale classification, or as Cavalier-Smith puts it [56], mega-classification, of prokaryotes, deals with higher taxonomic ranks such as phylum, class, and order (at present, ranks higher than order are not covered by the International Bacterial Code [57]).
Simultaneously, they can also be carried out with other libraries, such as LIBLINER [ 29], which is alternative for SVM classification, especially appropriate for large-scale classification problems.
These more robust approaches enabled large scale comparisons and classification of structural relatives.
However, none of these approaches has been used for large-scale sub-classification of all known protein domain superfamilies.
In "A Large-Scale Structural Classification of Antimicrobial Peptides," C.-C. Lee et al. presented a database of antimicrobial peptides (abbreviated as ADAM) which contains 7,007 unique sequences and 759 structures.
The structural classification data and large scale comparisons of domain structures also revealed novel folding motifs (split beta alpha beta motifs) common to a large proportion of alpha beta domain superfamilies in which structures comprise a central antiparallel beta-sheet covered by a layer of alpha-helices (alpha beta-plait folds [48]).
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