FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2030241439> ?p ?o ?g. }

• W2030241439 endingPage "5621" @default.
• W2030241439 startingPage "5617" @default.
• W2030241439 abstract "The kinetics of the Asp racemization in two model peptides, that is, (Asp-Leu)15 and (Leu-Asp-Asp-Leu)8-Asp, which form a β-sheet structure and an α-helix structure, respectively, have been investigated. The β-sheet structure protects against racemization. Biologically uncommon D-aspartyl (D-Asp) residues have been detected in proteins of various tissues of elderly humans. The presence of D-Asp has been explained as a result of the racemization of L-Asp (denoted as Asp) in the protein of inert tissues. We have previously suggested that the racemization of Asp may depend on the conformation of the peptide chain. However, the nature of the peptide conformation that affects the D-Asp formation has not yet been examined. Here we report the kinetics of Asp racemization in two model peptides, (Asp-Leu)15 and (Leu-Asp-Asp-Leu)8-Asp, which form β-sheet structures and α-helical structures, respectively. For the β-sheet structures, the activation energy of racemization of Asp residues was 27.3 kcal mol−1, the racemization rate constant at 37 °C was 2.14×10−2 per year and the time required to reach a D/L ratio of 0.99 at 37 °C was 122.6 years as estimated from the Arrhenius equation. For the α-helical structures, the activation energy of racemization was 18.4 kcal mol−1, the racemization rate constant 20.02×10−2 per year and the time 13.1 year. These results suggest that Asp residues inserted in α-helical peptides are more sensitive to racemization than Asp residues inserted in peptides adopting β-sheet structures. The results clearly indicate that the racemization rate of Asp residues in peptides depends on the secondary structure of the host peptide. Les acides aminés non biologiques D-aspartyl (D-Asp) ont été trouvés dans les protéines de divers tissus âgés. La présence de D-Asp a été attribuée à la racémisation de L-Asp dans les tissus inertes. Précédemment, nous avons suggéré que la racémisation de L-Asp dépendait de la conformation de la chaîne peptidique, sans toutefois avoir examiné la nature de la chaîne peptidique affectant la racémisation. Ici, nous décrivons la cinétique de racémisation de résidus L-Asp insérés dans deux peptides modèles, (Asp-Leu)15 et (Leu-Asp-Asp-Leu)8-Asp, qui adoptent respectivement une structure en feuillets-β et en hélice-α. L′énergie d′activation de la racémisation de L-Asp est de 27.3 kcal mol−1 pour (Asp-Leu)15 et de 18.4 kcal mol−1 pour (Leu-Asp-Asp-Leu)8-Asp. La constante de vitesse de racémisation à 37 °C est de 20.02×10−2 par an pour (Asp-Leu)15 et de 2.14×10−2 par an pour (Leu-Asp-Asp-Leu)8-Asp. Enfin, le temps nécessaire pour atteindre un rapport D/L de 0.99 à 37 °C est de 122.6 ans pour (Asp-Leu)15 et de 13.1 ans pour (Leu-Asp-Asp-Leu)8-Asp. Les résultats montrent que les résidus L-Asp insérés dans des peptides α-hélicoïdaux sont racémisés plus facilement que les mêmes acides aminés insérés dans des feuillets-β. Ils montrent ainsi que la racémisation des résidus Asp dans une chaîne peptidique dépend étroitement de la conformation du peptide." @default.
• W2030241439 created "2016-06-24" @default.
• W2030241439 creator A5041490444 @default.
• W2030241439 creator A5065647772 @default.
• W2030241439 creator A5066934733 @default.
• W2030241439 date "2007-06-25" @default.
• W2030241439 modified "2023-10-11" @default.
• W2030241439 title "Conformation-Dependent Racemization of Aspartyl Residues in Peptides" @default.
• W2030241439 cites W1611690919 @default.
• W2030241439 cites W1894503089 @default.
• W2030241439 cites W1898812238 @default.
• W2030241439 cites W1975427169 @default.
• W2030241439 cites W1975437978 @default.
• W2030241439 cites W1977727600 @default.
• W2030241439 cites W1983073430 @default.
• W2030241439 cites W1985036467 @default.
• W2030241439 cites W2000349942 @default.
• W2030241439 cites W2010766679 @default.
• W2030241439 cites W2013959518 @default.
• W2030241439 cites W2025609047 @default.
• W2030241439 cites W2035927542 @default.
• W2030241439 cites W2042238384 @default.
• W2030241439 cites W2061269546 @default.
• W2030241439 cites W2071019479 @default.
• W2030241439 cites W2088089099 @default.
• W2030241439 cites W2108689038 @default.
• W2030241439 cites W2497467692 @default.
• W2030241439 cites W3031163498 @default.
• W2030241439 cites W4238136596 @default.
• W2030241439 doi "https://doi.org/10.1002/chem.200601677" @default.
• W2030241439 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/17373006" @default.
• W2030241439 hasPublicationYear "2007" @default.
• W2030241439 type Work @default.
• W2030241439 sameAs 2030241439 @default.
• W2030241439 citedByCount "11" @default.
• W2030241439 countsByYear W20302414392015 @default.
• W2030241439 countsByYear W20302414392016 @default.
• W2030241439 countsByYear W20302414392018 @default.
• W2030241439 countsByYear W20302414392020 @default.
• W2030241439 crossrefType "journal-article" @default.
• W2030241439 hasAuthorship W2030241439A5041490444 @default.
• W2030241439 hasAuthorship W2030241439A5065647772 @default.
• W2030241439 hasAuthorship W2030241439A5066934733 @default.
• W2030241439 hasConcept C121332964 @default.
• W2030241439 hasConcept C148898269 @default.
• W2030241439 hasConcept C185592680 @default.
• W2030241439 hasConcept C18903297 @default.
• W2030241439 hasConcept C2778530040 @default.
• W2030241439 hasConcept C2779281246 @default.
• W2030241439 hasConcept C2779965526 @default.
• W2030241439 hasConcept C55493867 @default.
• W2030241439 hasConcept C60002323 @default.
• W2030241439 hasConcept C62520636 @default.
• W2030241439 hasConcept C71240020 @default.
• W2030241439 hasConcept C86803240 @default.
• W2030241439 hasConcept C93391505 @default.
• W2030241439 hasConceptScore W2030241439C121332964 @default.
• W2030241439 hasConceptScore W2030241439C148898269 @default.
• W2030241439 hasConceptScore W2030241439C185592680 @default.
• W2030241439 hasConceptScore W2030241439C18903297 @default.
• W2030241439 hasConceptScore W2030241439C2778530040 @default.
• W2030241439 hasConceptScore W2030241439C2779281246 @default.
• W2030241439 hasConceptScore W2030241439C2779965526 @default.
• W2030241439 hasConceptScore W2030241439C55493867 @default.
• W2030241439 hasConceptScore W2030241439C60002323 @default.
• W2030241439 hasConceptScore W2030241439C62520636 @default.
• W2030241439 hasConceptScore W2030241439C71240020 @default.
• W2030241439 hasConceptScore W2030241439C86803240 @default.
• W2030241439 hasConceptScore W2030241439C93391505 @default.
• W2030241439 hasIssue "19" @default.
• W2030241439 hasLocation W20302414391 @default.
• W2030241439 hasLocation W20302414392 @default.
• W2030241439 hasLocation W20302414393 @default.
• W2030241439 hasLocation W20302414394 @default.
• W2030241439 hasOpenAccess W2030241439 @default.
• W2030241439 hasPrimaryLocation W20302414391 @default.
• W2030241439 hasRelatedWork W1996521394 @default.
• W2030241439 hasRelatedWork W2088431388 @default.
• W2030241439 hasRelatedWork W2134664135 @default.
• W2030241439 hasRelatedWork W2413520336 @default.
• W2030241439 hasRelatedWork W2765723203 @default.
• W2030241439 hasRelatedWork W2949676535 @default.
• W2030241439 hasRelatedWork W2952110918 @default.
• W2030241439 hasRelatedWork W3021310309 @default.
• W2030241439 hasRelatedWork W3138279926 @default.
• W2030241439 hasRelatedWork W4253885752 @default.
• W2030241439 hasVolume "13" @default.
• W2030241439 isParatext "false" @default.
• W2030241439 isRetracted "false" @default.
• W2030241439 magId "2030241439" @default.
• W2030241439 workType "article" @default.