FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W286382405> ?p ?o ?g. }

• W286382405 abstract "Author(s): Diedrich, Jolene | Advisor(s): Julian, Ryan R | Abstract: Photodissociation (PD) mass spectrometry has been shown to be a useful analytical technique for determining protein modifications. Described herein is the development and application of photodissociation for various modifications. Photo-excitation with 266nm laser light normally does not yield fragmentation. However C-S, S-S, C-I, C-Br, and C-Cl bonds can be homolytic cleaved through direct dissociation pathways. This selective fragmentation can be utilized to identify peptides or proteins of interest. Radicals generated through this process can cause further dissociation of the peptide backbone. Radical directed dissociation (RDD) is useful for identifying the location of modification sites. The selective nature of fragmentation is shown to provide facile identification of PTM sites by greatly simplifying data analysis. Reported herein is the discovery of a novel gas phase dissociation technique useful for the facile analysis of protein modifications. Phosphorylation sites are selectively modified through â elimination and Michael addition chemistry, installing photolabile group. Photodissociation yields homolytic cleavage of the C-S bond at the modification site, generating a â radical which is poised to fragment the peptide backbone selectively at the previously phosphorylated residue, thus allowing facile identification. Cysteine residues, uniquely reactive amino acids, are shown to form covalent bonds with quinones. Furthermore, the chromophoric properties can be leveraged for site specific photodissociation. Photodissociation reveals both the presence and location of modified cysteine residues. Selective fragmentation of a single bond in a whole protein is demonstrated. PD can be used to determine both the presence and site of modification generated by naturally occurring molecules, such as dopamine, which can harness quinone chemistry to modify proteins.Also reported is the discovery of photodissociation at 266 nm to selectively cleave disulfide bonds in the gas phase, while leaving all other bonds intact. This methodology can be used to identify disulfide bonded pairs in complex systems. LC-MS experiments utilizing photodissociation were developed for analysis of protein digests. Peptides containing biomarkers of oxidative stress can be easily identified by LC-PD-MS. Proteins exposed to oxidative stress can be halogenated at tyrosine residues. Homolytic cleavage of the carbon-halogen bond is a favorable process and allows facile identification of these types of biomarkers. Shown in this dissertation is the selectivity offered by photodissociation; homolytic cleavage allows simplification of data analysis by quickly identifying the peptides of interest in a mixture while subsequent selective backbone fragmentation allows facile analysis of protein modifications." @default.
• W286382405 created "2016-06-24" @default.
• W286382405 creator A5030590878 @default.
• W286382405 date "2011-01-01" @default.
• W286382405 modified "2023-09-27" @default.
• W286382405 title "Harnessing Radical Chemistry for the Facile Identification of Post Translational Modification Sites in Proteins by Photodissociation Mass Spectrometry" @default.
• W286382405 cites W2159290811 @default.
• W286382405 hasPublicationYear "2011" @default.
• W286382405 type Work @default.
• W286382405 sameAs 286382405 @default.
• W286382405 citedByCount "0" @default.
• W286382405 crossrefType "journal-article" @default.
• W286382405 hasAuthorship W286382405A5030590878 @default.
• W286382405 hasConcept C102931765 @default.
• W286382405 hasConcept C111919701 @default.
• W286382405 hasConcept C139066938 @default.
• W286382405 hasConcept C161790260 @default.
• W286382405 hasConcept C162356407 @default.
• W286382405 hasConcept C175689099 @default.
• W286382405 hasConcept C178790620 @default.
• W286382405 hasConcept C180577832 @default.
• W286382405 hasConcept C181199279 @default.
• W286382405 hasConcept C185592680 @default.
• W286382405 hasConcept C191015642 @default.
• W286382405 hasConcept C21951064 @default.
• W286382405 hasConcept C2776982924 @default.
• W286382405 hasConcept C2779201268 @default.
• W286382405 hasConcept C2779281246 @default.
• W286382405 hasConcept C3044715 @default.
• W286382405 hasConcept C31684184 @default.
• W286382405 hasConcept C31827203 @default.
• W286382405 hasConcept C36674120 @default.
• W286382405 hasConcept C41008148 @default.
• W286382405 hasConcept C43617362 @default.
• W286382405 hasConcept C54582936 @default.
• W286382405 hasConcept C55493867 @default.
• W286382405 hasConcept C75473681 @default.
• W286382405 hasConceptScore W286382405C102931765 @default.
• W286382405 hasConceptScore W286382405C111919701 @default.
• W286382405 hasConceptScore W286382405C139066938 @default.
• W286382405 hasConceptScore W286382405C161790260 @default.
• W286382405 hasConceptScore W286382405C162356407 @default.
• W286382405 hasConceptScore W286382405C175689099 @default.
• W286382405 hasConceptScore W286382405C178790620 @default.
• W286382405 hasConceptScore W286382405C180577832 @default.
• W286382405 hasConceptScore W286382405C181199279 @default.
• W286382405 hasConceptScore W286382405C185592680 @default.
• W286382405 hasConceptScore W286382405C191015642 @default.
• W286382405 hasConceptScore W286382405C21951064 @default.
• W286382405 hasConceptScore W286382405C2776982924 @default.
• W286382405 hasConceptScore W286382405C2779201268 @default.
• W286382405 hasConceptScore W286382405C2779281246 @default.
• W286382405 hasConceptScore W286382405C3044715 @default.
• W286382405 hasConceptScore W286382405C31684184 @default.
• W286382405 hasConceptScore W286382405C31827203 @default.
• W286382405 hasConceptScore W286382405C36674120 @default.
• W286382405 hasConceptScore W286382405C41008148 @default.
• W286382405 hasConceptScore W286382405C43617362 @default.
• W286382405 hasConceptScore W286382405C54582936 @default.
• W286382405 hasConceptScore W286382405C55493867 @default.
• W286382405 hasConceptScore W286382405C75473681 @default.
• W286382405 hasLocation W2863824051 @default.
• W286382405 hasOpenAccess W286382405 @default.
• W286382405 hasPrimaryLocation W2863824051 @default.
• W286382405 hasRelatedWork W1699600831 @default.
• W286382405 hasRelatedWork W1983743164 @default.
• W286382405 hasRelatedWork W2015151985 @default.
• W286382405 hasRelatedWork W2023476162 @default.
• W286382405 hasRelatedWork W2106296216 @default.
• W286382405 hasRelatedWork W2112060212 @default.
• W286382405 hasRelatedWork W2164561625 @default.
• W286382405 hasRelatedWork W2170572834 @default.
• W286382405 hasRelatedWork W2404335790 @default.
• W286382405 hasRelatedWork W2417122937 @default.
• W286382405 hasRelatedWork W2523580724 @default.
• W286382405 hasRelatedWork W2581837667 @default.
• W286382405 hasRelatedWork W2588598264 @default.
• W286382405 hasRelatedWork W2736105822 @default.
• W286382405 hasRelatedWork W2736140192 @default.
• W286382405 hasRelatedWork W2795922219 @default.
• W286382405 hasRelatedWork W2910246843 @default.
• W286382405 hasRelatedWork W3021663797 @default.
• W286382405 hasRelatedWork W3087765001 @default.
• W286382405 hasRelatedWork W1475033597 @default.
• W286382405 isParatext "false" @default.
• W286382405 isRetracted "false" @default.
• W286382405 magId "286382405" @default.
• W286382405 workType "article" @default.