Theoretical study of the neuromedin U-8 (NmU-8) neuropeptide from porcine spinal cord

The spatial organization and conformational properties of the neuromedin U-8 (NmU-8) neuropeptide from porcine spinal cord have been established by the method of molecular mechanics. The conformational states corresponding to the local minimum of the whole molecule potential energy are obtained. The backbone structure comprises a type II b-turn formed by residues Arg5-Pro6-Arg7-Asn8. A large flexibility of the Tyr1-Phe2-Leu3-Phe4 amino acids sequence in contrast to other segment of the molecule was observed. q 2004 Elsevier B.V. All rights reserved