Abstract
A synthetic peptide Ala-Gln-Arg-Pro-Gln-Asp-Glu-Asn encephalitogenic
in the Lewis rat has been studied in aqueous solutions by 1H and 13C
n.m.r. The configuration about the Arg-Pro peptide bond
is > 99% trans. The temperature dependences and titration shifts of NH
resonances areconsistent with occurrence
of a number of intramolecular hydrogen bonds, leading to an unusually compact
structure for a linear peptide in aqueous solution.
Cited by
3 articles.
订阅此论文施引文献
订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献