Download Analyzing Biomolecular Interactions by Mass Spectrometry by Jeroen Kool, Wilfried M. A. Niessen PDF
By Jeroen Kool, Wilfried M. A. Niessen
This monograph studies all proper applied sciences according to mass spectrometry which are used to review or monitor organic interactions regularly.
prepared in 3 components, the textual content starts by means of reviewing concepts these days virtually thought of classical, reminiscent of affinity chromatography and ultrafiltration, in addition to the most recent innovations. the second one half focusses on all MS-based tools for the examine of interactions of proteins with all periods of biomolecules. along with pull down-based methods, this part additionally emphasizes using ion mobility MS, capture-compound methods, chemical proteomics and interactomics. The 3rd and ultimate half discusses different vital applied sciences usually hired in interplay stories, similar to biosensors and microarrays.
For pharmaceutical, analytical, protein, environmental and biochemists, in addition to these operating in pharmaceutical and analytical laboratories.
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Additional info for Analyzing Biomolecular Interactions by Mass Spectrometry
In MS1, a precursor ion is selected, mostly the protonated or deprotonated molecule of the target analyte. The selected ion is subjected to dissociation in the collision cell. In MS2, a preferably structure-speciﬁc product ion of the selected precursor is selected and detected. Thus, an SRM transition is a combination of a precursor ion m/z, a product ion m/z, and all MS parameters, for example, collision energy, required to measure this transition with the best sensitivity in a particular TQ instrument.
For a known elemental composition, the nitrogen rule allows discriminating between OE+• and EE+ ions. Another useful tool is the double-bond equivalent (DBE), “degree of unsaturation,” or “ring double bond” (RDB) parameter. The DBE can be calculated from the elemental composition of the molecule of ion, using the equation: 1 1 DBE = 1 + C– (H + F + Cl + Br + I) + (N + P) 2 2 The DBE is a measure of the number of unsaturations in the molecule, that is, the number of rings and/or double bonds. 5 for an EE+ ion.
Competition experiments could be performed as well by adding an excess of a high-aﬃnity inhibitor to the electrosprayed solution. 7) . This approach was coined “bioaﬃnity characterization mass spectrometry” . It basically comprises three steps: (i) selective accumulation of a noncovalent protein–ligand complex, (ii) gas-phase dissociation of the complex to release the ligand, and (iii) fragmentation of the ligand for further structure elucidation . 8 Orbitrap-Based Hybrid Systems Although stand-alone orbitrap systems have been produced, the full power of the orbitrap mass analyzer is achieved by its use in an MS–MS setting.