Spatial Structure of Peptide ВАМ-20Р


Authors : E.M. Hasanov, N.A. Akhmedov.

Volume/Issue : Volume 3 - 2018, Issue 3 - March

Google Scholar : https://goo.gl/DF9R4u

Scribd : https://goo.gl/FWyupG

Thomson Reuters ResearcherID : https://goo.gl/3bkzwv

Abstract : The spatial structure of the molecule Tyr1-Gly2-Gly3-Phe4-Met5-Arg6-Arg7-Val8-Gly9-Arg10Pro11-Glu12-Trp13-Trp14-Met15-Asp16-Tyr17-Gln18-Lys19 Arg20 (BAM 20P – bovin adrenal medulla 20 residue peptide) fragmentally studied by theoretical conformational analysis and it is shown that its spatial structure can be represented by 11 stable conformations falling in the energy interval 0-10 kcal/mol. The values of the dihedral angles of the main and side chains are found, the energy of intra- and interstitial interactions is estimated.

Keywords : Opioid peptides, ВАМ–20Р, spatial structure, molecule, conformation.

The spatial structure of the molecule Tyr1-Gly2-Gly3-Phe4-Met5-Arg6-Arg7-Val8-Gly9-Arg10Pro11-Glu12-Trp13-Trp14-Met15-Asp16-Tyr17-Gln18-Lys19 Arg20 (BAM 20P – bovin adrenal medulla 20 residue peptide) fragmentally studied by theoretical conformational analysis and it is shown that its spatial structure can be represented by 11 stable conformations falling in the energy interval 0-10 kcal/mol. The values of the dihedral angles of the main and side chains are found, the energy of intra- and interstitial interactions is estimated.

Keywords : Opioid peptides, ВАМ–20Р, spatial structure, molecule, conformation.

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