Collision-induced dissociation (CID) of peptides and proteins. Wells, J. M. & McLuckey, S. A. Methods Enzymol, 402:148–185, 2005.
doi  abstract   bibtex   
The most commonly used activation method in the tandem mass spectrometry (MS) of peptides and proteins is energetic collisions with a neutral target gas. The overall process of collisional activation followed by fragmentation of the ion is commonly referred to as collision-induced dissociation (CID). The structural information that results from CID of a peptide or protein ion is highly dependent on the conditions used to effect CID. These include, for example, the relative translational energy of the ion and target, the nature of the target, the number of collisions that is likely to take place, and the observation window of the apparatus. This chapter summarizes the key experimental parameters in the CID of peptide and protein ions, as well as the conditions that tend to prevail in the most commonly employed tandem mass spectrometers.
@Article{wells05collision-induced,
  author    = {J. Mitchell Wells and Scott A. McLuckey},
  title     = {Collision-induced dissociation ({CID}) of peptides and proteins.},
  journal   = {Methods Enzymol},
  year      = {2005},
  volume    = {402},
  pages     = {148--185},
  abstract  = {The most commonly used activation method in the tandem mass spectrometry (MS) of peptides and proteins is energetic collisions with a neutral target gas. The overall process of collisional activation followed by fragmentation of the ion is commonly referred to as collision-induced dissociation (CID). The structural information that results from CID of a peptide or protein ion is highly dependent on the conditions used to effect CID. These include, for example, the relative translational energy of the ion and target, the nature of the target, the number of collisions that is likely to take place, and the observation window of the apparatus. This chapter summarizes the key experimental parameters in the CID of peptide and protein ions, as well as the conditions that tend to prevail in the most commonly employed tandem mass spectrometers.},
  doi       = {10.1016/S0076-6879(05)02005-7},
  keywords  = {tandem ms},
  owner     = {rasche},
  pmid      = {16401509},
  timestamp = {13.02.2008},
}

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