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-NH 2 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 con...
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| Veröffentlicht in: | Biophysics (Oxford) 2013-07, Vol.58 (4), p.457-459 |
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| container_title | Biophysics (Oxford) |
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| creator | Gadjieva, Sh. N. Akhmedov, N. A. Masimov, E. A. Godjaev, N. M. |
| description | The spatial structure of cardioactive Thr-Pro-Ala-Glu-Asp-Phe-Met-Arg-Phe-NH
2
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. |
| doi_str_mv | 10.1134/S0006350913040052 |
| format | Article |
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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.</description><identifier>ISSN: 0006-3509</identifier><identifier>EISSN: 1555-6654</identifier><identifier>DOI: 10.1134/S0006350913040052</identifier><language>eng</language><publisher>Boston: Springer US</publisher><subject>Amino acids ; Biological and Medical Physics ; Biophysics ; Molecular Biophysics ; Peptides ; Physics ; Physics and Astronomy</subject><ispartof>Biophysics (Oxford), 2013-07, Vol.58 (4), p.457-459</ispartof><rights>Pleiades Publishing, Inc. 2013</rights><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c2312-298e2abec0745d869c792a63af2340eebc7f7679aebd08361720055e793fa8c63</citedby><cites>FETCH-LOGICAL-c2312-298e2abec0745d869c792a63af2340eebc7f7679aebd08361720055e793fa8c63</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1134/S0006350913040052$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1134/S0006350913040052$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,27922,27923,41486,42555,51317</link.rule.ids></links><search><creatorcontrib>Gadjieva, Sh. N.</creatorcontrib><creatorcontrib>Akhmedov, N. A.</creatorcontrib><creatorcontrib>Masimov, E. A.</creatorcontrib><creatorcontrib>Godjaev, N. M.</creatorcontrib><title>Spatial structure of Thr-Pro-Ala-Glu-Asp-Phe-Met-Arg-Phe-NH2 molecule</title><title>Biophysics (Oxford)</title><addtitle>BIOPHYSICS</addtitle><description>The spatial structure of cardioactive Thr-Pro-Ala-Glu-Asp-Phe-Met-Arg-Phe-NH
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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.</description><subject>Amino acids</subject><subject>Biological and Medical Physics</subject><subject>Biophysics</subject><subject>Molecular Biophysics</subject><subject>Peptides</subject><subject>Physics</subject><subject>Physics and Astronomy</subject><issn>0006-3509</issn><issn>1555-6654</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNp1kM1Lw0AQxRdRsFb_AG8Bz6uz39ljKLUVqhZaz2G7nfSDtIm7ycH_von1IIinGXjv94Z5hNwzeGRMyKcFAGihwDIBEkDxCzJgSimqtZKXZNDLtNevyU2MewAmQaoBGS9q1-xcmcQmtL5pAyZVkSy3gc5DRbPS0UnZ0izWdL5F-ooNzcLme3-b8uRQlejbEm_JVeHKiHc_c0g-nsfL0ZTO3icvo2xGPReMU25T5G6FHoxU61Rbbyx3WriCCwmIK28Ko411uFpDKjQzvHtFobGicKnXYkgezrl1qD5bjE2-r9pw7E7mTEqmOyS1nYudXT5UMQYs8jrsDi585Qzyvq38T1sdw89M7LzHDYZfyf9CJ3hmaFw</recordid><startdate>201307</startdate><enddate>201307</enddate><creator>Gadjieva, Sh. 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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.</abstract><cop>Boston</cop><pub>Springer US</pub><doi>10.1134/S0006350913040052</doi><tpages>3</tpages></addata></record> |
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| language | eng |
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| subjects | Amino acids Biological and Medical Physics Biophysics Molecular Biophysics Peptides Physics Physics and Astronomy |
| title | Spatial structure of Thr-Pro-Ala-Glu-Asp-Phe-Met-Arg-Phe-NH2 molecule |
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