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- W789047399 endingPage "6244" @default.
- W789047399 startingPage "6227" @default.
- W789047399 abstract "The objective of the present research is to explore the potential of an additional feature of proton 1D-NMR for the study of the properties of peptides in aqueous solution, namely the magnetic non-equivalence of N-methylene protons in linear acyclic peptides induced by an asymmetric carbon atom located nearby. For this exploratory study, we have chosen an l-Alanyl terminal residue adjacent to a Glycyl residue, itself grafted to an optically inactive terminal Histamine unit, i.e., the Histamine-containing pseudopeptide l-Alanyl-Glycyl-Histamine (AGHA). The pH- and temperature-dependence of magnetic non-equivalences of Glycyl and Histamine N-methylene protons was modeled as a weighted mean over four ionization states BH3, BH2, BH, B of AGHA molecules found in the pH range explored: pH −0.78 to 12. In parallel, this research has made it possible to assess the pK's governing the speciation curve, the base- and acid-catalyzed proton exchange rates and the pK's of amide bonds." @default.
- W789047399 created "2016-06-24" @default.
- W789047399 creator A5010631014 @default.
- W789047399 creator A5016211923 @default.
- W789047399 creator A5036889173 @default.
- W789047399 date "2015-09-01" @default.
- W789047399 modified "2023-10-18" @default.
- W789047399 title "Magnetic non-equivalence and dynamic NMR of N-methylene protons in a Histamine-containing pseudopeptide: Alanyl-Glycyl-Histamine" @default.
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