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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

Variable-Temperature ESI-IMS-MS Analysis of Myohemerythrin Reveals Ligand Losses, Unfolding, and a Non-Native Disulfide Bond.

TL;DR: The high-fidelity of IMS-MS techniques provides a means of examining the stabilities of individual components of complex mixtures that are inaccessible by traditional calorimetric and spectroscopic methods.
Journal ArticleDOI

Influence of acid-induced conformational variability on protein separation in reversed phase high performance liquid chromatography

TL;DR: The results suggest a pore exclusion induced separation related to protein conformation, which is influenced by the pH and type of acid used, and is likely to involve ion-pair formation.
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Advanced mass spectrometry-based methods for the analysis of conformational integrity of biopharmaceutical products.

TL;DR: The two particularly promising methods that are likely to have the most significant and lasting impact in many areas of biopharmaceutical analysis, direct ESI MS and hydrogen/deuterium exchange, are focus of this article.
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Gas-Phase Analysis of the Complex of Fibroblast GrowthFactor 1 with Heparan Sulfate : A Traveling Wave Ion Mobility Spectrometry (TWIMS) and Molecular Modeling Study

TL;DR: This work examined the effect of size and sulfation pattern of HS upon FGF1 oligomerization, binding stoichiometry and conformational stability, through a combination of ion mobility (IM) and theoretical modeling approaches, and demonstrated that certain tetrasaccharide-length fragments are also capable of inducing dimerization of FGF 1.
Journal ArticleDOI

Charge state distribution shifting of protein ions observed in matrix-assisted laser desorption ionization mass spectrometry.

TL;DR: A significant shift to lower mass-to-charge values can be obtained for many protein samples by using a new sample preparation method for matrix-assisted laser desorption ionization.
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