[Spatial structure of Thr-Pro-Ala-Glu-Asp-Phe-Met-Arg-Phe-NH2 molecule].
The spatial structure of cardioactive Thr-Pro-Ala-Glu-Asp-Phe-Met-Arg-Phe-NH2 molecule has been investigated using a theoretical conformational analysis. The low-energy conformations of the molecule were found, the values of the backbone and side T-T chain dihedral angles of amino acid residues constituting the peptide were determined, and the energies of intra- and interresidual interactions were estimated. It is revealed that the spatial structure of this molecule can exist in 11 stable backbone forms.
Sh N
ShN
Gadzhieva
N A
NA
Akhmedov
É A
ÉA
Masimov
N M
NM
Godzhaev
D000596:Amino Acids / Q000737:chemistry*; D019835:FMRFamide / Q000737:chemistry*; D008958:Models, Molecular; D011487:Protein Conformation; D011498:Protein Precursors / Q000737:chemistry*; D013816:Thermodynamics
D000596:Amino Acids; D011498:Protein Precursors; C121688:threonyl-prolyl-alanyl-glutamyl-aspartyl-phenylalnyl-methionyl-arginyl-phenylalanylamide; D019835:FMRFamide