ArticleJournal of the American Society for Mass Spectrometry2009
Rapid peptide fragmentation without electrons, collisions, infrared radiation, or native chromophores.
Article in Journal of the American Society for Mass Spectrometry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
9 citing papers in PubMed.
- Comprehensive Overview of Bottom-Up Proteomics Using Mass Spectrometry.ACS measurement science au · 2024Review
- Article
- Coupling 193 nm Ultraviolet Photodissociation and Ion Mobility for Sequence Characterization of Conformationally-Selected Peptides.Journal of the American Society for Mass Spectrometry · 2020Article
- Glycomics and glycoproteomics of viruses: Mass spectrometry applications and insights toward structure-function relationships.Mass spectrometry reviews · 2020Review
- Initial Protein Unfolding Events in Ubiquitin, Cytochrome c and Myoglobin Are Revealed with the Use of 213 nm UVPD Coupled to IM-MS.Journal of the American Society for Mass Spectrometry · 2019Article
- The Mechanism Behind Top-Down UVPD Experiments: Making Sense of Apparent Contradictions.Journal of the American Society for Mass Spectrometry · 2017Article
- Ion Activation Methods for Peptides and Proteins.Analytical chemistry · 2016Review
- Structural and energetic effects in the molecular recognition of acetylated amino acids by 18-crown-6.Journal of the American Society for Mass Spectrometry · 2012Article
- Ultraviolet photodissociation of carboxylate-derivatized peptides in a quadrupole ion trap.Journal of the American Society for Mass Spectrometry · 2011Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ultraviolet photodissociation of peptides followed by mass analysis has several desirable advantages relative to other methods, yet it has not found widespread use due to several limitations. One shortcoming is the inefficiency with which peptides absorb in the ultraviolet. This issue has a simple solution and can be circumvented by the attachment of noncovalent adducts that contain appropriate chromophores. Subsequent photoactivation of the chromophore leads to vibrational excitation of the complex and eventually to fragmentation of the peptide. Herein, the energetics that control the efficiency of this process are examined as a function of the characteristics of both the peptide and the noncovalently attached chromophore. Fragmentation efficiency decreases with increasing peptide size and is also constrained by the binding energy of the noncovalent adduct. The optimum chromophore should have excellent absorption at the excitation wavelength and a low luminescence quantum yield. It is demonstrated that a naphthyl based 18-crown-6 adduct is ideally suited for attaching to a variety peptides and fragmenting them following absorption of 266 nm light. Potential applications and limitations of this methodology are discussed.
Indexed as
Identifiers
19036607What OpenQuestion holds
Registered trials
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.