Abstract
A series of terminally blocked peptides consisting of tetrapeptide repeat. Boc-Asn-Ala-(Asn-Pro-Asn-Ala) n-0,1,2,5,17 -Asn-Pro-OBzl, has been synthesized and one and two dimensional 1 H NMR studies in dimethyl sulfoxide (Me 2 SO)-d 6 as well as distance geometry calculations have been carried out. The repeating tetrapeptidc units constitute the central area of the circumsporozoite coat protein of human malaria parasite Pkrsmodium falciparum. The two dimensional nuclear Overhauser effect (NOE) data observed in Me 2 SO and the information from the temperature dependence of the amide proton chemical shifts were used as constraints in distance geometry calculations. The result suggests that each -(Asn-Pro-Asn-Ala)- tetrapeptide forms a structural unit, a considerable population of which exists as unique turnlikc structurcs.
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