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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

Solvent effect on analyte charge state, signal intensity, and stability in negative ion electrospray mass spectrometry; implications for the mechanism of negative ion formation.

TL;DR: Chloroform is a recommended solvent for negative ion electrospray mass spectrometry (ES/MS) when solubility is not a limiting issue and solvent polarity was shown to exhibit a profound influence on the distribution of charge states in negative ion ES/MS.
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Review of a current role of mass spectrometry for proteome research

TL;DR: This review is intended to give readers a snapshot of current mass spectrometry for proteomics research to cover a brief history of mass Spectrometry proteomic research, peptidomics and proteomics for biomarker search, quantitative proteomics, proteomics with post-translational modification and future perspective of proteomics.
Journal ArticleDOI

Effect of Solution Ionic Strength on Analyte Charge State Distributions in Positive and Negative Ion Electrospray Mass Spectrometry

TL;DR: In this article, the variability of ESMS charge state distributions was investigated for a number of analytes when the ionic strength of their solutions was altered over a wide range, including NH 4 OAc, CsCl, or (n-C 4 H 9 ) 4 N + Cl - ) to protein solutions.
Journal ArticleDOI

High Accuracy Molecular Weight Determination and Variation Characterization of Proteins Up To 80 ku by Ionspray Mass Spectrometry

TL;DR: A quadrupole mass spectrometer with an ionspray interface was used to measure the molecular weight (MW) of proteins up to 80,000 u and revealed that the two minor ones had lost amino acid residues Ser and Ser-Asp, respectively, from the major component.
Journal ArticleDOI

Origin of supercharging in electrospray ionization of noncovalent complexes from aqueous solution

TL;DR: The results indicate that the enhanced charging upon addition of m-NBA to aqueous electrospray solutions is a result of droplet heating owing to the high boiling point ofm-NBA, which results in a change in the higher-order structure and/or dissociation of the complexes.
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