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Cited by 300

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Primary Sequence Information from Intact Proteins by Electrospray Ionization Tandem Mass Spectrometry

Loo, Joseph A., Edmonds, Charles G., Smith, Richard D.·1990·Science

Abstract

Tandem mass spectrometry has been used to obtain information related to portions of the primary sequence for an intact protein, bovine ribonuclease A. Multiply charged molecular ions, generated by electrospray ionization, were collisionally dissociated at low energies in a triple quadrupole mass spectrometer to yield singly and multiply charged fragment ions that can be assigned to the known sequence of the protein. Dissociation of the highly charged molecular ions resulted in pairs of complementary product ions. The higher order (gas-phase) protein structure affects the dissociation processes, as observed in comparisons of tandem mass spectra of the native and disulfide-reduced forms of ribonuclease A.

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Crossref · 10.1126/science.2326633

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Metadata

Authors
Loo, J. A., Edmonds, C. G., & Smith, R. D.
Venue
Science
Published
1990-04-13
Volume
248
Issue
4952
Pages
201-204
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2023887263
Cited by
300
References
1
FWCI
11.63
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Primary Sequence Information from Intact Proteins by Electrospray Ionization Tandem Mass Spectrometry. https://app.cochat.ai/papers/10.1126/science.2326633
The paper
Loo, J. A., Edmonds, C. G., & Smith, R. D. (1990). Primary Sequence Information from Intact Proteins by Electrospray Ionization Tandem Mass Spectrometry. Science. https://doi.org/10.1126/science.2326633

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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.