Detection and localization of protein modifications by high resolution tandem mass spectrometry

• Published in: Mass spectrometry reviews 2005-03, Vol.24 (2), p.126-134
• Main Authors: Meng, Fanyu, Forbes, Andrew J., Miller, Leah M., Kelleher, Neil L.
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Analytical, structural and metabolic biochemistry; Biological and medical sciences; FTMS; Fundamental and applied biological sciences. Psychology; General aspects, investigation methods; Mass Spectrometry - methods; Molecular Sequence Data; MS/MS; post-translational modification; Proteins; Proteins - analysis; Proteins - chemistry; Spectroscopy, Fourier Transform Infrared
• ISSN: 0277-7037; 1098-2787
• DOI: 10.1002/mas.20009

For interrogation of peptides with diverse modifications, no other instrument is as versatile as the Fourier‐transform mass spectrometer (FTMS). Particularly using electrospray ionization (ESI), many intact proteins and their proteolytic products harboring post‐translational and chemical modifications (PTMs) have been studied by high resolution tandem mass spectrometry (MS/MS). The widely touted analytical figures of merit for FTMS in fact have translated into clarity when analyzing PTMs from phosphorylations to disulfides, oxidations, methylations, acetylations, and even exotic PTMs found in the biosynthesis of antibiotics and other natural products. A top down approach to PTM detection and localization is proving extensible to an increasing variety of PTMs, some of which are stable to MS/MS at the protein level but unstable to amide bond cleavage by threshold dissociations at the level of small peptides