Brenda L. Schwartz

TL;DR: Differences in the relative stabilities of these tetrameric proteins, formed from the known solution structures, are qualitatively consistent with the gas-phase stability observed with ESI-MS by adjusting the atmosphere-vacuum interface conditions.

TL;DR: The work demonstrates that ESI-MS has significant potential for measuring relative binding affinities and characterizing the structures of ligands associated noncovalently to proteins and should be widely useful in medicinal chemistry.

TL;DR: The ability of ESI-MS to estimate simultaneously the relative binding affinities of a protein to soluble ligands in a library, if general, should be useful in drug development.

TL;DR: An extended mass-to-charge ratio range quadrupole mass spectrometer was employed to examine the effects of harsher conditions in the ESI atmosphere-vacuum interface region on the streptavidin tetramer.

TL;DR: Electrospray ionization mass spectrometry was used to investigate the structure of the Escherichia coli chaperone protein SecB and it was determined that the N‐terminal methionine of SecB has been removed and that more than half of all SecB monomers are additionally modified, most likely by acetylation of the N-terminus or a lysine.