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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

On-line hollow-fiber flow field-flow fractionation-electrospray ionization/time-of-flight mass spectrometry of intact proteins.

TL;DR: Correlation between the molar mass values independently measured by HF FlFFF retention and ESI/TOFMS allows us to confirm the protein aggregation features of bovine serum albumin and to indicate possible changes in the quaternary structure of human hemoglobin.
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The gas phase structure of coulombically stretched polyethylene glycol ions.

TL;DR: All sharp shape transitions observed at decreasing ion mass involve ejection of one elementary charge from the shrinking globule into the growing linear appendage, supported by molecular dynamics simulations and approximate calculations of electrical mobilities for computed structures.
Journal ArticleDOI

Noncovalent protein tetramers and pentamers with "n" charges yield monomers with n/4 and n/5 charges.

TL;DR: Results from the gas-phase dissociation of protein-protein complexes upon collision into a surface demonstrate that alternative subunit fragments, not observed through multiple collisions with gas atoms, can be generated through surface collision.
Journal ArticleDOI

Extending mass spectrometry contribution to therapeutic monoclonal antibody lead optimization: characterization of immune complexes using noncovalent ESI-MS.

TL;DR: Investigations focused on mAb:Ag complexes revealed that, similarly to murine mAb, humanized mAb 6F4 binds selectively up to four antigen molecules with a similar affinity, confirming in this way the reliability of the humanization process.
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Electrothermal supercharging of proteins in native electrospray ionization.

TL;DR: In this article, the formation of high charge-state protein ions with nanoelectrospray ionization (nESI) from purely aqueous ammonium bicarbonate solutions at neutral pH, where the proteins have native or native-like conformations prior to ESI droplet formation, is demonstrated.
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