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Journal ArticleDOI

Probing conformational changes in proteins by mass spectrometry

Swapan K. Chowdhury, +2 more
- 21 Nov 1990 - 
- Vol. 112, Iss: 24, pp 9012-9013
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.

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Journal ArticleDOI

Charge‐state distributuion and electric‐discharge suppression in negative‐ion electrospray mass spectrometry using/chlorinated solvents

TL;DR: In this article, the authors examined solvent effects in electrospray mass spectrometry performed in the negaative-ion mode, for a series of low-nucleophilicity chlorinated solvents.
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MALDI mass spectrometry of dye-peptide and dye-protein complexes.

TL;DR: It is proved that the interaction between dye-protein and dye-peptide complexes is prodominantly electrostatic and that it involves protonated sites of the peptides and proteins, including the NH2 terminus, and deprotonated SO3 groups of the dyes.
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Gas-phase processes and measurements of macromolecular properties in solution: On the possibility of false positive and false negative signals of protein unfolding

TL;DR: In this paper, the effect of gas phase processes on mass measurement (e.g., integrity of macromolecular complexes in the absence of solvent, non-specific interactions, etc.), the focus of attention is the ionic charge.
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Gas Phase Stability of Protein Ions in a Cyclic Ion Mobility Spectrometry Traveling Wave Device.

TL;DR: Investigation of protein ion stability using a multipass traveling wave (TW) cyclic IM (cIM) device and the geometry of the instrument provides unique capabilities with the potential to expand the field of protein analysis via IM-MS.
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Solid-state glycation of β-lactoglobulin monitored by electrospray ionisation mass spectrometry and gel electrophoresis techniques

TL;DR: The charge state distribution data obtained by ESI-MS indicated that adduct formation with lactose, but more significantly galactose, tends to improve the stability properties of the native protein towards denaturation.
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