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The proteasomal cleavage tools predict potential cleavage sites or most probable peptide fragments.
As such, we now consider the problem of finding the most probable peptide π=π1, …,π n for a set of multiple (possibly overlapping) spectra s, …, s k.
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First, the amino acid sequence of the cyclin B1 protein was screened for the most probable HLA-A2 nonameric peptide epitopes using different CTL epitope prediction algorithms.
Although the technical limitations of proteomics analyses are among the most probable reason for detecting peptides for <60% of the protein-coding genes, there may be another reason for not identifying peptides for certain genes.
NetPhos prediction indicated that most probable TRP47 phosphorylated residues were Y44 (peptide 41 49) and S159 and/or S161 (peptide 147 163).
In the present work, we investigate the ability of continuum approaches to predict the most probable orientation of the β-hairpin antimicrobial peptide Protegrin-1 (PG-1) in DLPC lipid bilayers by calculating the difference in the transfer free energy from an aqueous environment to a membrane-water environment for multiple orientations.
For each sequence the probability value to contain a signal peptide was considered alongside the most probable position for the cleavage site.
We report the probability of the most probable path for each of the equally probable gene segment sets.
MALDI-TOF MS/MS spectrometry analysis of trypsin-digested peptides from purified supernatants from all recombinant P. pastoris, determined that none of the most probable or de novo amino acid sequence of the evaluated peptide fragments matched the expected amino acid sequence of the bacteriocins SRCAM 602, OR-7, E-760, and L-1077 (Table 5).
The set of most probable values for the angles defines the low energy conformation of the peptide.
Probability ranges from 1 10, with 10 being the most probable.
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