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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

Electrospray ionization mass spectrometry and hydrogen/deuterium exchange for probing the interaction of calmodulin with calcium.

TL;DR: The extent of H/D exchange of protein calmodulin in solution was monitored by mass spectrometry following electrospray ionization (ESI) of the protein this article.
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Characterization of cytochrome c variants with high-resolution FTICR mass spectrometry: correlation of fragmentation and structure

TL;DR: These studies demonstrate that electrospray ionization-FTICR using SORI-CID can be a useful tool to probe not only the small differences in the primary sequences of proteins but also suggest the potential for probing their higher-order structures and yielding information not readily available from H/D exchange or circular dichoism studies.
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Total chemical synthesis of enzymatically active human type II secretory phospholipase A2

TL;DR: It is demonstrated that chemical synthesis of sPLA2 yields a fully active native-like enzyme and offers a straightforward tool to provide s PLA2 analogs for structure-activity studies of anticoagulant, lipolytic, or inflammatory activities.
Journal ArticleDOI

On the Formation of Highly Charged Gaseous Ions from Unfolded Proteins by Electrospray Ionization

TL;DR: A bead chain model is used for examining how charge is partitioned as protein and droplet separate, and it is shown that protein ejection from differently sized ESI droplets generates a range of protonation states.
Journal ArticleDOI

Impact of Different Wort Boiling Temperatures on the Beer Foam Stabilizing Properties of Lipid Transfer Protein 1

TL;DR: The results presented here show that LTP1 denaturation reduces its ability to act as a binding protein for foam-damaging FFA, and suggest that wort boiling temperature is an important factor in determining the level and conformation of LTP 1, thereby favoring satisfactory beer foam stability.
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