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The heavy arginine is incorporated into newly synthesized proteins, resulting in a 10-Da mass shift between new and old histone peptides.
The EpiTYPER® software identifies methylated versus unmethylated CGs based on detection of a 16-Dalton mass shift between the two peaks.
Structures of potential metabolite candidates were assigned based on retention times, mass shift between theoretical mass and observed mass (<5 ppm), peak abundance and fragmentation pattern.
Each peptide should appear as a pair, differing only in the mass shift between the two samples with light versus heavy amino acids, and this ratio of peak intensities represents the ratio of the amount of each protein.
Although potentially straightforward, this quantitative strategy can be hampered by the overlap of isotopic clusters of light and heavy peaks, which occurs whenever the mass shift between the peptide pairs is smaller than their isotopic envelope.
If the substance was found in our samples the mass shift between no label and full label was identified for multiple fragments per substance using the GMD (http://gmd.mpimp-golm.mpg.de/).
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Mass spectral peaks of biological origin were identified manually by searching for mass shifts between C- and C-mass spectra.
Mass spectral peaks of biological origin were identified manually by searching for mass shifts between the C and C mass spectra.
M and M H+ differ in mass by one hydrogen (1.007825032 Da) minus an electron (0.000548625 Da); in Fig. 8c this difference is decomposed into a mass shift of one (see the shift between the mass axes) and an additional small mass spacing Δ m = 0.000233878 Da.
The mass shift of a PTM is the mass difference between the modified form (with the PTM) and the unmodified form of an amino acid residue.
Crosslinks between Ser/Thr and Lys/His/Cys were searched using a mass shift of −18.01051 Da due to the elimination of H2O during crosslink formation.
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