Utilization of MALDI-TOF Mass Spectrometry for Study of Spatial Structure of Proteins

Authors

  • V. Kadlcik Department of Environmental Chemistry, Institute of Chemical Technology, Prague
  • M. Kodicek Department of Environmental Chemistry, Institute of Chemical Technology, Prague
  • M. Hassman Department of Environmental Chemistry, Institute of Chemical Technology, Prague

Abstract

MALDI-TOF MS, a technique developed in the late 1980's, is today a routine method for detection and identification of proteins but its utilization for study of spatial structure of proteins is ever-growing.. The main approaches are detection of chemical and post-translational modifications of proteins, characterization of protein structure by proteolysis, detection of protium-deuterium ion exchange, characterization of the disulfide structure of proteins and direct detection of non-covalent complexes. MALDI-TOF is thus the technique that can replace some much more time-consuming and experimentally demanding methods but it can also afford information inaccessible by other methods.

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Published

2002-08-15

How to Cite

Kadlcik, V., Kodicek, M., & Hassman, M. (2002). Utilization of MALDI-TOF Mass Spectrometry for Study of Spatial Structure of Proteins. Chemické Listy, 96(7). Retrieved from http://www.chemicke-listy.cz/ojs3/index.php/chemicke-listy/article/view/2317

Issue

Vol. 96 No. 7 (2002)

Section

Articles