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Cited by 453

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Conformational changes in proteins probed by hydrogen‐exchange electrospray‐ionization mass spectrometry

Katta, Viswanatham, Chait, Brian T., Carr, Steven·1991·Rapid Communications in Mass Spectrometry

Abstract

Hydrogen‐exchange electrospray‐ionization mass spectrometry is demonstrated to be an effective new method for probing conformational changes of proteins in solutions. The method is based on the mass spectrometric measurement of the extent of hydrogen/deuterium exchange that occurs in different protein conformers over defined periods of time. Results are presented in which hydrogen‐exchange electrospray‐ionization mass spectrometry is used to probe conformational changes in bovine ubiquitin induced by the addition of methanol to aqueous acidic solutions of the protein.

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Metadata

Authors
Katta, V., Chait, B. T., & Carr, S.
Venue
Rapid Communications in Mass Spectrometry
Publisher
Wiley
Published
1991-04
Volume
5
Issue
4
Pages
214-217
ISSN
  • 0951-4198 (ISSN-L)
  • 1097-0231
OpenAlex
W2115463031
Cited by
453
References
1
FWCI
12.80
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Conformational changes in proteins probed by hydrogen‐exchange electrospray‐ionization mass spectrometry. https://app.cochat.ai/papers/10.1002/rcm.1290050415
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Katta, V., Chait, B. T., & Carr, S. (1991). Conformational changes in proteins probed by hydrogen‐exchange electrospray‐ionization mass spectrometry. Rapid Communications in Mass Spectrometry. https://doi.org/10.1002/rcm.1290050415

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.