TITLE

MİOMODULİN F MOLEKULUNUN FƏZA QURULUŞU

AUTHOR(S)
Əhmǝdov, N. A.; Abbasli, R. M.; İsmayilova, L. İ.
PUB. DATE
March 2011
SOURCE
Journal of Qafqaz University;2011, Issue 31, p44
SOURCE TYPE
Academic Journal
DOC. TYPE
Article
ABSTRACT
Myomodulin molecules belonging to the family of neuropeptides influence the flow of neurotransmitters in neurons and mebranes. Using the method of theoretical conformational analysis the spatial structure of the heptapeptide molecule myomodulin F with the amino acid sequence Ser1-Leu2-Asn3-Met4-Leu5-Arg6-Leu7-NH2 was investigated. Calculation of the heptapeptide molecule's potential energy was carried out taking into account the energy of non-valent, electrostatic and torsional interactions, as well as energy of hydrogen bonds. The spatial structure of the molecule myomodulin F was determined in fragments. In the first phase we found conformational features of two tetrapeptides: N-terminal tetrapeptide Ser1-Leu2-Asn3-Met4 and C-terminal tetrapeptide Met4-Leu5-Arg6-Leu7-NH2. The results of the spatial structure's calculations of two tetrapeptides allowed determining the spatial structure of the whole heptapeptide molecule. Conformational fragmental analysis indicates that spatial structure of this molecule can be described by set of 9 stable backbone forms. For each low-energy spatial structures energy contributions to interresidual interactions, as well as values of dihedral angles of the main and side chains of aminoacids within the molecule have been found.
ACCESSION #
73352249

 

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