Electrospray ionization mass spectrometry: a promising new technique in the study of protein/DNA noncovalent complexes.
With the emergence of electrospray ionization mass spectrometry (ESI-MS), mass spectrometry is no longer restricted to the study of small, stable molecules, but has become a viable technique to study large biomolecules as well as noncovalent biomolecular complexes. ESI-MS has been used to study noncovalent interactions involving proteins with metals, ligands, peptides, oligonucleotides, and other proteins. An area where ESI-MS holds significant promise is in the study of protein/DNA interactions. The most common technique employed to study protein/DNA interactions is the electrophoretic gel mobility shift assay (EMSA). Although this technique has and will continue to provide excellent results, ESI-MS has shown the ability to provide detailed results not easily obtainable by EMSA. In this review I will discuss some of the protein/DNA noncovalent interactions that have been measured using ESI-MS, and contrast the results obtained by ESI-MS to those obtained by EMSA.
Veenstra
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Pacific Northwest National Laboratory, Richland, Washington 99352, USA. timothy.veenstra@pnl.gov
D004247:DNA / Q000737:chemistry / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000378:metabolism*; D004583:Electrons; D007477:Ions; D013058:Mass Spectrometry / Q000379:methods; D011485:Protein Binding
D004268:DNA-Binding Proteins; D007477:Ions; D004247:DNA