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Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
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Different notations are used to represent the three-dimensional structure of molecules on two-dimensional surfaces. One of the most commonly used representations is the dash-wedge formula. The dashed wedges, solid wedges, and the plane lines indicate the groups situated behind the plane, coming out of the plane, and in the plane, respectively.
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Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

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[Spatial structure of isoleucine pentapeptides Glu-Phe-Leu-Arg-Ile-NH2 and Pro-Phe-Tyr-Arg-Ile-NH2].

Biofizika·2008
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[Spatial structure of the cardioactive octapeptide].

Biofizika·2008
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[Structure-function organization of neurokinin A and neurokinin B molecules. III. A conformational study of glycine-monosubstituted analogues of neurokinins A and B].

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[Spatial structure of BAM-12P dodecapeptide and its analogues].

Bioorganicheskaia khimiia·2005
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[The structure-function organization of neurokinin A and neurokinin B molecules. II. Theoretical conformational analysis of neurokinin B].

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[Tertiary structure of myelopeptides. II. Conformational analysis of Phe-Arg-Pro-Arg-Ile-Met-Thr-Pro, Val-Val-Tyr-Pro-Asp, and Val-Asp-Pro-Pro].

Bioorganicheskaia khimiia·2005
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Related Experiment Video

Updated: May 3, 2026

Förster Resonance Energy Transfer Mapping: A New Methodology to Elucidate Global Structural Features
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[Spatial structure of Thr-Pro-Ala-Glu-Asp-Phe-Met-Arg-Phe-NH2 molecule].

Sh N Gadzhieva, N A Akhmedov, É A Masimov

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    |January 25, 2014
    PubMed
    Summary
    This summary is machine-generated.

    Theoretical conformational analysis revealed 11 stable backbone structures for the cardioactive Thr-Pro-Ala-Glu-Asp-Phe-Met-Arg-Phe-NH2 peptide. This peptide conformational study provides insights into its spatial arrangement and interactions.

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    Area of Science:

    • Biochemistry and Molecular Modeling
    • Peptide Chemistry
    • Structural Biology

    Context:

    • Understanding the spatial structure of biologically active peptides is crucial for drug design and molecular mechanism elucidation.
    • Cardioactive peptides play significant roles in physiological processes, necessitating detailed structural investigation.
    • Theoretical conformational analysis offers a powerful approach to explore peptide structures in silico.

    Purpose:

    • To investigate the spatial structure of the cardioactive peptide Thr-Pro-Ala-Glu-Asp-Phe-Met-Arg-Phe-NH2.
    • To identify low-energy conformations and determine dihedral angles of the peptide backbone and side chains.
    • To estimate intra- and interresidual interaction energies.

    Summary:

    • A theoretical conformational analysis was performed on the cardioactive peptide Thr-Pro-Ala-Glu-Asp-Phe-Met-Arg-Phe-NH2.
    • Low-energy conformations were identified, and backbone/side chain dihedral angles were determined.
    • The study revealed that the peptide can exist in 11 stable backbone forms, with insights into interaction energies.

    Impact:

    • Provides fundamental structural data for the cardioactive peptide, aiding in understanding its function.
    • The identification of multiple stable conformations suggests potential for diverse biological activities.
    • This research contributes to the broader field of peptide structure-activity relationship studies.