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In order to investigate the effects of amino acid similarity on the bilinear regression analysis, we used the similarity matrix to score the sequence alignments based on structure, and defined percent sequence non-similarity (PNS) in a similar way with PNI.
Additionally, we used the BLOSUM62 amino acid substitution matrix to score alignments between evolutionarily divergent protein sequences.
Poorly aligning positions were detected and removed with BMGE (Criscuolo and Gribaldo 2010) using the BLOSUM30 matrix to score conservation.
Atias and Sharan proposed a diffusion process in the ADR similarity matrix to score each ADR by assuming that similar ADRs receive similar scores.
It is also necessary to upload a transition matrix to score the following nucleotides as well as the probabilities in the real model (TP) and the expected probabilities in the random or background model (TQ).
The program accepts a multiple sequence alignment of protein sequences as input and employs a DAYHOFF-type amino acid exchange matrix to score amino acid replacements for every pair of sequences.
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We used the generalized linear model framework to analyze repeated outcome measurements and used an unstructured covariance matrix to account for correlations in scores within individuals.
By encoding RNA and protein sequences into numeric vectors, we used matrix multiplication to score each RNA protein pair.
A BLOSUM62 (Blocks Substitution Matrix) matrix is used to score the match of each residue pair in these three residue-long alignments (Henikoff and Henikoff, 1992).
A BLOSUM62 (Blocks Substitution Matrix) matrix is used to score the match of each residue pair in these three residue-long alignments (Henikoff and Henikoff, 1992 ). To exclude spurious matches composed solely of hydrophobic residues, the cumulative score for the three residues must be >12.
This study utilized four scoring matrices and one scoring matrix to calculate the binding scores of peptide-MHC (which is similar to protein-protein interface (PPI)) and TCR-peptide (which is similar to antigen-antibody (Ag-Ab) [ 20, 21]) interfaces, respectively.
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