In proteomics, proteolytic peptides are often chemically modified to improve MS analysis, peptide identification, and/or to enable protein/peptide quantification. It is known that such chemical modifications can alter peptide fragmentation in collision induced dissociation MS/MS. Here, we investigated the fragmentation
Use of triethlammonium buffers in ion-exchange chromatography and electrophoresis.
The separation of 5'-adenosine di- and triphosphates from inorganic pyrophosphate or imidodiphosphate can be accomplished with reverse-phase HPLC by using a solvent system buffered by triethylammonium bicarbonate (pH 6.7). This buffer was used because it was neutral, readily volatile at
Journal of mass spectrometry : JMS, 35(7), 870-877 (2000-08-10)
The applicability of ion-pair reversed-phase high-performance liquid chromatography/electrospray ionization mass spectrometry (IP-RP-HPLC/ESI-MS) and direct infusion/ESI-MS to the characterization of nucleic acid mixtures was evaluated by the analysis of the reaction products obtained from solid-phase synthesis of a 39-mer oligonucleotide. IP-RP-HPLC/ESI-MS
Hypothetical (HyP) and conserved HyP genes account for >30% of sequenced bacterial genomes. For the sulfate-reducing bacterium Desulfovibrio vulgaris Hildenborough, 347 of the 3634 genes were annotated as conserved HyP (9.5%) along with 887 HyP genes (24.4%). Given the large
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