![CONFORMATIONAL ANALYSIS NEUROPEPTIDE [HYP2]MET-CALLATOSTATIN](/upload/21232f297a57a5a743894a0e4a801fc3/journals/cover/f8c56688fa307e98584d30b341015d28.jpeg)
In work by the method of molecular mechanics in approximation of atom-atom potential functions is studied the spatial structure and conformational properties of the neuropeptide from allatostatin family, got the name of [Hyp2]Met-callatostatin. The researches were based on minimizing of the energy of intramolecular interactions ( non- bonded, electrostatic, torsion ) in the vicinity of the internal rotation angles corresponding to all combinations of stable conformations of monopeptide residues forming a molecule. There determined ten energetically stable conformations of neuropeptide, implemented under the conditions of implicitly given aqueous environment , the relative conformational energy of which varies in the range of 0-10 kcal / mol. It was shown that the system of hydrogen bonds, despite a small contribution to the total energy of the molecule is essential for the preservation of a stable structure and restriction of [Hyp2]Met-callatostatin . According to the research results, the main contribution to the stabilization of low-energy conformations of the molecule are made by non - valentinteractions.
neyropeptides, structures, conformational analysis
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