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Recently, peptide mass mapping using MALDI TOF MS (Matrix-Assisted Laser Desorption/Ionization – Time of Flight Mass Spectrometry) was shown to be an effective tool for protein analysis in such challenging insoluble materials as historical mortars.
Finally, proteins were separated prior to their identification by peptide mass mapping using MALDI-TOF MS and bioinformatics.
Digested samples were analyzed by peptide mass mapping using reversed phase chromatography with in-line UV (214 nm) and electrospray ionization with mass spectrometric detection (LC-ESI-MS).
Indeed, peptide mass mapping using both trypsin and Asp-N in gel digestion revealed that the C-terminal tryptic peptide Val327 - Asn356 was present in Nit-ANigRec but absent in Nit-ANigWT.
For the identification of induced hemolymph proteins, tryptic digests were performed, peptide mass mapping using MALDI-TOF mass spectrometry was carried out, and de novo sequencing of peptides conducted by nano LC-MS/MS.
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LysC peptide mapping using MALDI-TOF mass spectrometry shows that UV-induced damage to ALDH3A1 also includes chemical modifications to Trp, Met, and Cys residues.
The resulting peptide mass maps were used to interrogate S. aureus MRSA252 sequences to generate statistically significant candidate identifications using the MASCOT search engine (Matrix Science).
The spots were excised from the gels and peptide mass mapping was performed using a PerSeptive Biosystems Voyager-DE STR mass spectrometer.
Interactions of mammalian mIF3 with the ribosome have been mapped using chemical cross-linking followed by mass-spectrometry [47].
Transcription termination sites were mapped using 3' RACE.
All reads were mapped using Maq.
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