ArticleJournal of the American Society for Mass Spectrometry2017
From Compact to String-The Role of Secondary and Tertiary Structure in Charge-Induced Unzipping of Gas-Phase Proteins.
Article in Journal of the American Society for Mass Spectrometry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
5 citing papers in PubMed.
- Characterization of the Protein Corona of Three Chairside Hemoderivatives on Melt Electrowritten Polycaprolactone Scaffolds.International journal of molecular sciences · 2023Article
- Chondroitin Sulfate Disaccharides in the Gas Phase: Differentiation and Conformational Constraints.The journal of physical chemistry. A · 2021Article
- Article
- A new azobenzene-based design strategy for detergents in membrane protein research.Chemical science · 2020Article
- Glycosaminoglycan Analysis by Cryogenic Messenger-Tagging IR Spectroscopy Combined with IMS-MS.Analytical chemistry · 2017Article
Corrections and comments
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Authors and funding
6 authors.
Funding
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Abstract
In the gas phase, protein ions can adopt a broad range of structures, which have been investigated extensively in the past using ion mobility-mass spectrometry (IM-MS)-based methods. Compact ions with low number of charges undergo a Coulomb-driven transition to partially folded species when the charge increases, and finally form extended structures with presumably little or no defined structure when the charge state is high. However, with respect to the secondary structure, IM-MS methods are essentially blind. Infrared (IR) spectroscopy, on the other hand, is sensitive to such structural details and there is increasing evidence that helices as well as β-sheet-like structures can exist in the gas phase, especially for ions in low charge states. Very recently, we showed that also the fully extended form of highly charged protein ions can adopt a distinct type of secondary structure that features a characteristic C
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.