LOW-ENERGY CONFORMATIONS OF DELICIOUS PEPTIDE, A FOOD FLAVOR - STUDY BY QUENCHED MOLECULAR-DYNAMICS AND NMR

NMR and quenched molecular dynamics investigations of Delicious Peptid e are reported. Four families of structures are derived from the molec ular dynamics simulation, which can be considered as cyclic, due to hy drogen bonding from the first residue to the end of the chain, or S-sh aped. The S-shaped family contains the lowest energy structures, which is consistent with the NMR results obtained. The families of structur es display interactions between the acidic and basic parts of the mole cule, which is consistent with the currently accepted theory for the f lavor-inducing properties of this peptide.