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- W2030303563 abstract "Abstract The ability of 15 N relaxation measurements in conformational analysis of linear peptides was studied using Leu-enkephalin: Tyr-★Gly-★Gly-★Phe-★Leu and and related tetrapeptide Tyr-★Gly-★Gly-★Phe 95 % 15 N enriched. 15 N spin-lattice relaxation times measured at different temperatures in Me 2 SO solution indicate the presence of highly preferential folded structures in both peptides. A marked dependence of T 1 upon the motional effects (segmental rather than anisotropic overall) was observed, while hydrogen bonding affects weakly the relaxation times. From a comparison of 15 N relaxation parameters it appears that the tetrapeptide exhibits a more rigid structure than Leu-enkephalin, in accordance with previous 1 H NMR studies. This paper provides evidence for the usefulness of 15 N T 1 as a mobility probe (independent from 13 C) in the investigation of the conformational dynamics of peptides." @default.
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- W2030303563 date "1981-08-01" @default.
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- W2030303563 title "15N spin-lattice relaxation study of linear peptides: Preliminary results on Leu-enkephalin and Tyr-Gly-Gly-Phe" @default.
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- W2030303563 doi "https://doi.org/10.1016/0006-291x(81)91809-x" @default.
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