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We present an analytical method using electrospray ionization-mass spectrometry (ESI-MS) that has none of the mentioned difficulties.
Hegeman et al. applied this method using electrospray ionization (ESI) liquid chromatography−mass spectrometry (LC−MS) and a deuterated methanol label also to determine the degree of phosphorylation.
We illustrate the application of our method using electrospray ionization liquid chromatography−mass spectrometry by quantifying phosphorylation of troponin I with protein kinase A and protein kinase C. The method also improves the retention and elution of hydrophilic peptides.
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This method used electrospray ionization (ESI) [179].
Recent advances in stable isotope labelling of surfactant phospholipids coupled with analytical methods using electrospray ionisation mass spectrometry enable highly specific molecular assessment of phospholipid subclasses and synthetic rates that can be utilised for phenotypic characterisation and individualisation of exogenous surfactant replacement therapy.
Most traditional LC/MS-MS methods use electrospray ionization (ESI) or atmospheric chemical ionization; however, PBDEs do not ionize well with either of these two techniques.
Proteomics users enjoy the rapid development of LC-MS-based label-free relative quantification methods but in practice these remain restricted to mass spectrometers using electrospray ionization.
Oligomeric species are identified using electrospray mass spectrometry.
Separated peptides were analyzed for mass using electrospray mass spectroscopy.
Mass spectrometry detection was achieved by using electrospray ionization.
The molecular mass of the peptide was determined to be 885 Da using electrospray ionization mass spectrometry, and the sequence was identified as Asp-Pro-Asp-Ala-Asp-IIe-Leu-Gln using the Edman degradation method.
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