| Abstract: | The conformational behavior of the active C-terminal heptapeptide of neurotensin (NT), Pro-Arg-Arg-Pro-Tyr-Ile-LeuOH, or NT{7–13}, was investigated using empirical energy calculations. A sequential approach was used to display the specific contribution of each residue to induce stable conformations of the whole heptapeptide. The most stable conformations include numerous conformations of various types in a rather limited energy range. There is no preferential conformation contrary to the active C-terminal pentapeptide. These structures may coexist in the biological environment. |
