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Therefore, the characterization of their peptide bond specificity is important for understanding the active site preference associated with effective proteolysis as well as for the design of peptide substrates and inhibitors.
Furthermore, characterization of their peptide bond specificity is of value for understanding active site preference of the proteinase associated with effective proteolysis as well as of use in the design of peptide substrates and inhibitor lead compounds.
In this study we used proteome derived peptide libraries in the Proteomic Identification of protease Cleavage Sites (PICS) approach to explore the peptide bond specificity of Bothrops protease A and PA-BJ in order to determine their individual peptide cleavage sequences.
In this study we use a large, plasma based, proteome-derived peptide library as substrates along with mass spectrometry to explore the peptide bond specificity of three PI SVMPs and one PIII SVMP to determine their individual peptide cleavage consensus sequences.
Our mass spectrometry data suggest that in analogy to presenilin, MCMJR1 displays promiscuous peptide bond specificity as processing of the chimeric substrates was shown to occur at multiple positions within the hydrophobic region of the predicted TMD.
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Different substrate and peptide bond specificities between the two isoforms have been previously described [13], and their differential activity towards E-cadherin corroborates the distinct functions of both subunits.
Typically the determination of peptide bond cleavage specificity of snake venom serine proteinases (SVSPs) and snake venom metalloproteinases (SVMPs) has been performed using limited sets of peptides or small oligopeptides as experimental substrates.
Because our structure-activity analyses showed that regions flanking the disulfide bond mediated specificity, we synthesized 18 novel OSCs by structural modification of the most promising dysoxysulfone derivatives.
These weak charges allow a DNA base and its complement to engage in the activity of forming hydrogen (weak polar) chemical bonds; the specificity of this activity is due to the topological arrangements of the weak polar charges in the subparts of the base.
The substrate Abz-SSIYSQTEEQ-EDDnp was cleaved at the Tyr-Ser bond with a specificity constant kcat/Km of 60 000 making1, makitg ithehe best substrate for hK3 described to date.
Further, switching the position of the cysteine and the methionine involved in the cross-link also abolished thioether bond formation, demonstrating specificity of SkfB for the directionality of the thioether linkage.
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