An Overview of Protein Mass Spectrometry

New mass spectrometric methods developed over the last several years have led to the establishment of mass spectrometry as a powerful technique for protein structure determination. Key to this development was the introduction of fast atom bombardment (FAB) ionization which permitted production of intact molecular ions from peptides and small proteins as well as from other labile biological molecules. Other ionization methods (electrospray ionization [ESI], matrix assisted laser desorption ionization [MALDI]) have subsequently been developed which have been demonstrated to permit measurement of protein molecular weights in excess of several hundred thousand daltons.

In combination with these new ionization methods, tandem mass spectrometry permits amino acid sequencing of peptide fragments of proteins as well as characterization of posttranslational modifications. Mass spectrometry therefore provides a means of determining the complete primary structure of a protein. Use of chemical modifications in conjunction with mass spectrometric analysis provides a means of gaining information on the three dimensional structure as well. The use of mass spectrometry in the study of the various aspects of protein structure is discussed in more detail on subsequent pages.

We are located in room 305 of the Children's Research Institute Building at MUSC.

Biomolecular Mass Spectrometry Facility Department of Pharmacology Medical University of South Carolina 173 Ashley Avenue, CRI 305 Charleston, SC 29425	Telephone Numbers: 843-792-5849 (CRI 305) 843-792-2471 (department office) FAX: 843-792-2475