[Spatial organization of the N-terminal beta-endorphin tridecapeptide].
Using conformational analysis spatial structure and conformational properties of the N-terminal tridecapeptide--endorphine molecules were investigated. Calculations were based on the fragmental analysis using non-valent, electrostatic, torsional interactions and hydrogen bonds. It was shown that tridecapeptide could exist in several low-energetical conformational states. Enkephaline fragments structure depends on the most perspective structure of free metioninenkephaline. The results can be used for conformational analysis of endorphine molecules, for structure--function relations study.
D004723:Endorphins; D009842:Oligopeptides; D010455:Peptides; D011487:Protein Conformation; D001615:beta-Endorphin
D004723:Endorphins; D009842:Oligopeptides; D010455:Peptides; D001615:beta-Endorphin
Prostranstvennaia organizatsiia N-kontsevogo tridekapeptida beta-éndorfina.