Abstract
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 β-turn formed by residues Arg 5-Pro 6-Arg 7-Asn 8. A large flexibility of the Tyr 1-Phe 2-Leu 3-Phe 4 amino acids sequence in contrast to other segment of the molecule was observed.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
