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
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Journal ArticleDOI
Co-populated Conformational Ensembles of β2-Microglobulin Uncovered Quantitatively by Electrospray Ionization Mass Spectrometry
TL;DR: By linear deconvolution of the charge state distributions, the extent to which each conformational ensemble is populated throughout the pH range can be determined and quantified and highlights the potential of electrospray ionization mass spectrometry to resolve and quantify complex mixtures of different conformational species.
Journal ArticleDOI
Salt Bridge Rearrangement (SaBRe) Explains the Dissociation Behavior of Noncovalent Complexes.
TL;DR: It is shown that collisionally-facilitated salt bridge rearrangement (SaBRe) may explain unusual size “contractions” seen for some activated, low charge state complexes, and that some low-charged multimers preferentially cleave covalent bonds or shed small ions to disrupting noncovalent associations is also explained by greater ion pairing in low chargeState complexes.
Journal ArticleDOI
The methanol-induced conformational transitions of β-lactoglobulin, cytochrome c, and ubiquitin at low pH: A study by electrospray ionization mass spectrometry
TL;DR: The methanol-induced conformational transitions under acidic conditions for β-lactoglobulin, cytochrome c, and ubiquitin, representing three different classes of proteins with β-sheets, α- helices, and both α-helices and β-sheet, respectively, are studied under equilibrium conditions by electrospray ionization mass spectrometry (ESI-MS.
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Effects of Ammonium Bicarbonate on the Electrospray Mass Spectra of Proteins: Evidence for Bubble-Induced Unfolding
TL;DR: The data imply that heat and bubbles act synergistically to cause unfolding during the electrospray process, while proteins reside in ESI droplets, and advise against the use of ammonium bicarbonate for native ESI-MS.
Journal ArticleDOI
Investigating solution-phase protein structure and dynamics by hydrogen exchange mass spectrometry.
TL;DR: In this unit, hydrogen exchange theory is discussed as it applies to Hx‐MS protocols, the practice of HX‐MS including data analysis and interpretation is explained in detail, and recent advancements in technology which greatly increase the depth of information gained from the technique are highlighted.
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