Journal ArticleDOI
Probing conformational changes in proteins by mass spectrometry
TLDR
The authors describe the first use of mass spectrometry for probing conformational changes in proteins in a manner analogous to that employed in techniques like optical rotary dispersion, circular dichroism, and spectrophotometry.Abstract:
Mass spectrometry has found wide application for the elucidation of the primary structures of proteins. However, with the exception of topographical studies of membrane-bound proteins, mass spectrometry has not previously been utilized to obtain information concerning in three-dimensional conformation of proteins. In the present communication, the authors describe the first use of mass spectrometry for probing conformational changes in proteins in a manner analogous to that employed in techniques like optical rotary dispersion, circular dichroism, and spectrophotometry.read more
Citations
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Journal ArticleDOI
Observation and implications of high mass-to-charge ratio ions from electrospray ionization mass spectrometry.
Brian E. Winger,Karen J. Light-Wahl,Rachel R. Ogorzalek Loo,Harold R. Udseth,Richard D. Smith +4 more
TL;DR: The observation that protein aggregates are formed with charge states comparable to monomeric species (at fower mass-to-charge ratios) suggests that the high mass- to-charge ratio monomers may be formed by the dissociation of aggregate species.
Journal ArticleDOI
Supercharging in electrospray ionization: effects on signal and charge
TL;DR: In this article, the authors show that the addition of either of two compounds, m -nitrobenzyl alcohol (m -NBA) or glycerol, to electrospray solutions results in an increase in the number of charges that can be added to gas-phase protein cations.
Journal ArticleDOI
Resolution and Structural Transitions of Elongated States of Ubiquitin
TL;DR: Activation of ions that exist in low-abundance conformations, having mobilities that fall in between sharp peaks associated with higher abundances species, shows that the low- abundance forms undergo efficient conversion into states associated with well-defined peaks.
Journal ArticleDOI
Mass spectrometry of ribosomes and ribosomal subunits
TL;DR: Nanoflow electrospray ionization has been used to introduce intact Escherichia coli ribosomes into the ion source of a mass spectrometer and the pattern of dissociation correlates strongly with predicted features of ribosomal protein-protein and protein-RNA interactions.
Journal ArticleDOI
Conformation of cytochrome c studied by deuterium exchange-electrospray ionization mass spectrometry.
TL;DR: Neither charge-state distribution nor deuterium exchange rate alone is a sufficient indicator of protein conformation, and the data suggest that at least two conformations can have identical charge- state distributions, but have different exchange rates.
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