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
Native ion mobility-mass spectrometry and related methods in structural biology.
TL;DR: This overview article will describe these methods and highlight some recent applications for proteins and protein complexes, with particular emphasis on native MS analysis.
Journal ArticleDOI
Supercharged protein and peptide ions formed by electrospray ionization.
TL;DR: This method of producing highly charged protein ions should be useful for improving the performance of mass measurements on mass spectrometers with performances that decrease with increasing m/z, and should also be particularly useful for tandem mass Spectrometry experiments, for which highly charged ions are desired.
Journal ArticleDOI
Electrospray mass spectrometry for protein characterization
Matthias Mann,Matthias Wilm +1 more
TL;DR: Physicists have solved the problems associated with vaporizing and ionizing proteins and peptides, thereby allowing mass spectrometry to take on new roles in investigating protein sequences, structures and modifications.
Journal ArticleDOI
Conformations, unfolding, and refolding of apomyoglobin in vacuum : an activation barrier for gas-phase protein folding
TL;DR: In this paper, gas-phase ion mobility measurements have been used to characterize the conformations of the +4 to +22 charge states of apomyoglobin, generated by electrospraying pH.
Journal ArticleDOI
Fast photochemical oxidation of protein footprints faster than protein unfolding.
TL;DR: Fast photochemical oxidation of proteins is applied to three oxidation-sensitive proteins and it is found that the distribution of modification (oxidation) states is Poisson when a scavenger is present, consistent with a single conformation protein modification model.
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