The utility of mass spectrometry for the analysis of proteins has grown eno
rmously in the past decade. Significant advances in detection and ionizatio
n techniques are allowing questions about noncovalent assembly to be addres
sed by the direct observation of gas phase complexes, their assembly in rea
l time and their disassembly by perturbation of solution or instrument cond
itions. These technological innovations have plainly captured the imaginati
on of biological researchers. Recent and novel developments include the com
bination of mass spectrometry with isotopic labeling, affinity labeling and
genomic information. Collectively, these advances are opening new doors to
the isolation of complexes, the identification of their substituents and t
he characterization of their conformations and assembly.