The dodecapeptide (RPP) is an active peptide, which we extracted from
chinese rape pollen. The dodecapeptide enhances the activity of TNF on
murine tumor cells and also shows immunopromotive activities. The pos
sible conformation of the RPP, which has been previously studied by ci
rcular dichroism, has been studied by one and two dimensional NMR spec
troscopy. All resonance assignments were made by use of two dimensiona
l correlation spectroscopy. The problem of sequential resonance assign
ments was solved by using two dimensional NOE spectroscopy. The dihedr
al angles of the amide planes of the RPP, were calculated from the mea
sured coupling constants using Karplus equation, The temperature coeff
icient and NOE in different solvents together suggest that RPP exists
mainly as random coil in aqueous solution and some sections in the RPP
exist as gamma-turn.