Biology Reference
In-Depth Information
without scanning for different ions to acquire a complete mass spec-
trum. TOF-TOF instruments combine the quasi-simultaneous
detection of all ions in TOF 1 with high-energy CID MS/MS of
selected ions for PMF identification of proteins from genome
sequenced organisms [ 57 ]. High sequence coverage achieved by the
high dynamic range of TOF-MS (Table 1 ), along with accurate mass
measurement coupled with sufficient resolution, makes it possible to
greatly restrict the number of false positives in protein database
searches. In addition, the high analytical speed and automation makes
MALDI-TOF-TOF MS suitable for large number of samples.
Despite the great sophistication of currently available configura-
tions, it is disappointing to note that there is no ideal mass spectrome-
try system capable of performing all applications required in proteomics
[ 94 ]. To complicate matters, the increasing trend of employing highly
automated mass spectrometry platforms in high-throughput
approaches is contributing to create numerous operators and users
who are unaware of the fundamentals of MS and for whom mass spec-
trometers are little more than black boxes able to produce thousands
of spectra per day in full computerized workflow. The objective pur-
sued by this chapter was to show that the basic operational principles of
mass spectrometry can be understood by a simple mathematical lan-
guage, and that this understanding is necessary to rationally utilizing
this versatile technique in its full potential. However, MS and MS/MS
spectra interpretation is outside the scope of this essay. The reader is
referred to several excellent monographs [ 95 - 100 ].
References
1. Gelpí E (2008) From large analogical instru-
ments to small digital black boxes: 40 years of
progress in mass spectrometry and its role in
proteomics. Part I 1965-1984. J Mass
Spectrom 43:419-435
2. Gelpí E (2008) From large analogical instru-
ments to small digital black boxes: 40 years of
progress in mass spectrometry and its role in
proteomics. Part II 1985-2000. J Mass
Spectrom 44:1137-1161
3. Thomson JJ (1897) Cathode rays. Philos
Mag 44:293 (consult also http://www-
outreach.phy.cam.ac.uk/camphy/electron/
electron_index.htm )
8. Downard KM (2007) Francis William
Aston—the man behind the mass spectro-
graph. Eur J Mass Spectrom 13:177-190
9. Paul W, Steinwedel H (1953) Ein neues
Massenspektrometer
ohne
Magnetfeld.
Zeitsch Naturforsch A8:448-450
10. Paul W (1990) Electromagnetic traps for
charged and neutral particles. Rev Mod Phys
62:531-540
11. Dehmelt HG (1989) Experiments with an
isolated subatomic particle at rest. Nobel lec-
ture ( http://www.nobelprize.org/nobel_
prizes/physics/laureates/1989/
dehmelt-lecture.pdf )
12. Miller PE, Denton MB (1986) The quadru-
pole mass filter: basic operating concepts. J
Chem Ed 63:617-622
13. Dawson PH (1986) Quadrupole mass analyz-
ers: performance, design and some recent
applications. Mass Spectrom Rev 5:1-37
14. Cooks RG, Glish GL, McLuckey SA et al
(1991) Ion trap mass spectrometry. Chem
Eng News 69:26-30
4. Wien K (1999) 100 years of ion beams: Willy
Wien's canal rays. Braz J Phys 29:401-414
5. Falconer I (2001) Corpuscles to electrons. In:
Buchwald J, Warwick A (eds) Histories of the
electron. MIT, Cambridge, MA, pp 77-100
6. Dempster AJ (1918) A new method of posi-
tive ray analysis. Phys Rev 11:316-325
7. Aston FW (1919) A positive ray spectrograph.
Philos Mag Ser 6(38):707-714
Search WWH ::




Custom Search