In the past mass spectrometry has been limited to the study of small, stabl
e molecules, however, with the emergence of electrospray ionization mass sp
ectrometry (ESI-MS) large biomolecules as well as non-covalent biomolecular
complexes can be studied. ESI-MS has been used to study non-covalent inter
actions involving proteins with metals, ligands, peptides, oligonucleotides
, as well as other proteins. Although complementary to other well-establish
ed techniques such as circular dichroism and fluorescence spectroscopy, ESI
-MS offers some advantages in speed, sensitivity, and directness particular
ly in the determination of the stoichiometry of the complex. One major adva
ntage is the ability of ESI-MS to provide multiple signals each arising fro
m a distinct population within the sample. In this review I will discuss so
me of the different types of non-covalent biomolecular interactions that ha
ve been studied using ESI-MS, highlighting examples which show the efficacy
of using ESI-MS to probe the structure of biomolecular complexes. (C) 1999
Elsevier Science B.V. All rights reserved.