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Advances in mass spectroscopy using the 'top-down' approach to proteomics, in which intact proteins are ionized directly without previous peptide fragmentation, are proving especially fruitful for PTM analysis, yielding greater mass accuracy than ever before.
Doses (100 μg) of SWCNTs were instilled into the airways of the IPRL and the pulmonary translocation of SWCNTs quantified by inductively coupled plasma mass spectroscopy using CNT-associated nickel as the probe.
The SNPs were genotyped by using primer extension of multiplex products with detection by matrix-assisted laser desorption ionization – time of flight mass spectroscopy using a MassARRAY Compact Analyzer (Sequenom, San Diego, CA, USA).
The Proteomics based tests assess patterns of protein or glycoprotein by mass spectroscopy using serum samples.
PBDEs (n = 65) were determined by electron capture negative ion (low resolution) mass spectroscopy using an external standard.
Genotyping was performed by matrix-assisted laser desorption/ionization time-of-flight mass spectroscopy using a MassARRAY platform.
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Traditional mass spectroscopy uses a magnetic field to bend the path of electrically charged molecules.
An electrochemically generated adsorbed product can be identified by FD-mass spectroscopy using a pure metal FD-emitter which can be utilized as the working electrode.
MIMOSA is a mass spectroscopy technique using stable isotopes to quantitatively measure the discrete rates of sequential individual reactions in glycolytic and mitochondrial metabolism.
Quantitation was performed by liquid chromatography and mass spectroscopy (LC−MS) using human insulin as a standard.
Mass spectroscopy was used to determine as to whether the sample contained the stated, or other API 33, 34 and the content measurements of each API was determined using high-performance liquid chromatography (HPLC).
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