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This research aims at showing that deciphering NMR patterns of peptide anisochronous methylene protons (A and B) coupled to an adjacent NH or CH(X) hydrogen may bring novel structural and dynamical information, using for this purpose four l-Histidine-containing peptides and the NMR patterns of Glycyl or β-Alanyl residues or of the Histidyl side-chain, or else of a grafted N-butyl chain. Investigations...
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...
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