Magic Numbers in Protein Structures

Per-Anker Lindgård, Henrik Bohr

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    Abstract

    A homology measure for protein fold classes has been constructed by locally projecting consecutive secondary structures onto a lattice. Taking into account hydrophobic forces we have found a mechanism for formation of domains containing magic numbers of secondary structures and multipla of these domains. We have performed a statistical analysis of available protein structures and found agreement with the predicted preferred abundances. Furthermore, a connection between sequence information and fold classes is established in terms of hinge forces between the structural elements.
    Original languageEnglish
    JournalPhysical Review Letters
    Volume77
    Issue number4
    Pages (from-to)779-782
    ISSN0031-9007
    DOIs
    Publication statusPublished - 1996

    Bibliographical note

    Copyright (1996) American Physical Society.

    Keywords

    • SECONDARY STRUCTURE
    • GLOBULAR-PROTEINS
    • STABILITY

    Cite this

    Lindgård, Per-Anker ; Bohr, Henrik. / Magic Numbers in Protein Structures. In: Physical Review Letters. 1996 ; Vol. 77, No. 4. pp. 779-782.
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    Magic Numbers in Protein Structures. / Lindgård, Per-Anker; Bohr, Henrik.

    In: Physical Review Letters, Vol. 77, No. 4, 1996, p. 779-782.

    Research output: Contribution to journalJournal articleResearchpeer-review

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    T1 - Magic Numbers in Protein Structures

    AU - Lindgård, Per-Anker

    AU - Bohr, Henrik

    N1 - Copyright (1996) American Physical Society.

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    N2 - A homology measure for protein fold classes has been constructed by locally projecting consecutive secondary structures onto a lattice. Taking into account hydrophobic forces we have found a mechanism for formation of domains containing magic numbers of secondary structures and multipla of these domains. We have performed a statistical analysis of available protein structures and found agreement with the predicted preferred abundances. Furthermore, a connection between sequence information and fold classes is established in terms of hinge forces between the structural elements.

    AB - A homology measure for protein fold classes has been constructed by locally projecting consecutive secondary structures onto a lattice. Taking into account hydrophobic forces we have found a mechanism for formation of domains containing magic numbers of secondary structures and multipla of these domains. We have performed a statistical analysis of available protein structures and found agreement with the predicted preferred abundances. Furthermore, a connection between sequence information and fold classes is established in terms of hinge forces between the structural elements.

    KW - SECONDARY STRUCTURE

    KW - GLOBULAR-PROTEINS

    KW - STABILITY

    U2 - 10.1103/PhysRevLett.77.779

    DO - 10.1103/PhysRevLett.77.779

    M3 - Journal article

    VL - 77

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    EP - 782

    JO - Physical Review Letters

    JF - Physical Review Letters

    SN - 0031-9007

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    ER -