The BioPharma Finder application supports the following fragmentation methods for mass spectral (MS) data:
Acronym | Name | Description |
|---|---|---|
CID | collision-induced dissociation | Molecular ions are accelerated to high kinetic energy in the vacuum of a mass spectrometer and then allowed to collide with neutral gas molecules such as helium, nitrogen, or argon. The collision breaks the bonds and fragments the molecular ions into smaller pieces. |
ETciD | electron transfer collision-induced dissociation | Hybrid ETD and CID fragmentation method, which involves an initial electron-transfer dissociation step and produces additional b and y ions. |
IR-ETciD | infrared-activated electron transfer collision-induced dissociation | Infrared-induced activation and desolvation coupled with the standard ETciD method. |
HCD | higher-energy collision-induced dissociation | Ion optics accelerate the precursor ions into a high-pressure cell, where they collide with nitrogen gas. The projectile ion has laboratory-frame translation energy higher than 1 keV. |
EThcD | electron transfer higher-energy collision dissociation | Hybrid ETD and HCD fragmentation method, which involves an initial electron-transfer dissociation step and produces additional b and y ions. |
IR-EThcD | infrared-activated electron transfer higher-energy collision dissociation | Infrared-induced activation and desolvation coupled with the standard EThcD method. |
ETD | electron transfer dissociation | Singly charged reagent anions transfer electrons to protonated peptides within an ion trap mass analyzer to induce fragmentation. ETD cleaves randomly along the peptide backbone, while side chains and modifications (such as phosphorylation), are left intact. This method is used to fragment peptides and proteins. |
IR-ETD | infrared-activated electron transfer dissociation | Infrared-induced activation and desolvation coupled with the standard ETD method. |
SID | surface-induced dissociation | Molecular ions collide with a target surface composed of a relatively rigid material to maximize fragmentation. |
ECD | electron capture dissociation | Protonated molecules are introduced to low-energy free electrons. Capture of the electrons releases electric potential energy and reduces the charge state of the ions by producing odd-electron ions, which easily fragment. |
IRMPD | infrared multi-photon dissociation | An infrared laser is directed at the ions in an ion trap mass analyzer. The precursor ions absorb multiple infrared photons until they reach more energetic states and begin to break bonds, resulting in b and y fragment ions. |
UVPD | ultraviolet photodissociation | Ultraviolet photons activate the proteins for fragmentation, providing ultra-high resolution for improved structural elucidation and quantitation of isobaric compounds. |
PTCR | proton transfer charge reduction | Multiply-charged ions transfer protons to a neutral, basic carrier gas, gently reducing the charge states and simplifying mass spectra without fragmenting the molecule, which is especially useful for top-down analysis of proteins. |