Proteins fulfill a plethora of biochemical functions within every living organism, and mass spectrometry (MS) has become one of the most powerful and popular modern physical-chemical methods to study the complexities of proteins. In particular, the invention of matrix-assisted laser desorption/ionization (MALDI)  and electrospray ionization (ESI) technologies[2, 3] allows one to measure protein molecular weights and sequences, and to probe conformations and post-translational modifications of proteins. In addition, the mass range of species amenable for MS analysis has increased, enabling the transfer of ionized non-covalent species with masses well over one million (e.g., 1.5 MDa 24-Mer flavoprotein vanillyl-alcohol oxidase (VAO) from Penicillium simplicissimum ) into the gas phase. These advances moved MS into the range of intact protein oligomers and functional machineries.
|Original language||English (US)|
|Title of host publication||Characterization of Protein Therapeutics using Mass Spectrometry|
|Number of pages||58|
|ISBN (Print)||1441978615, 9781441978615|
|State||Published - Oct 1 2013|
All Science Journal Classification (ASJC) codes