• myGriffith
    • Staff portal
    • Contact Us⌄
      • Future student enquiries 1800 677 728
      • Current student enquiries 1800 154 055
      • International enquiries +61 7 3735 6425
      • General enquiries 07 3735 7111
      • Online enquiries
      • Staff phonebook
    View Item 
    •   Home
    • Griffith Research Online
    • Book chapters
    • View Item
    • Home
    • Griffith Research Online
    • Book chapters
    • View Item
    JavaScript is disabled for your browser. Some features of this site may not work without it.

    Browse

  • All of Griffith Research Online
    • Communities & Collections
    • Authors
    • By Issue Date
    • Titles
  • This Collection
    • Authors
    • By Issue Date
    • Titles
  • Statistics

  • Most Popular Items
  • Statistics by Country
  • Most Popular Authors
  • Support

  • Contact us
  • FAQs
  • Admin login

  • Login
  • Predicting interaction sites between glycolytic enzymes and cytoskeletal proteins employing concepts of the Molecular Recognition Theory

    Author(s)
    Sheedy, RJ
    Clarke, FM
    Griffith University Author(s)
    Clarke, Francis M.
    Year published
    2001
    Metadata
    Show full item record
    Abstract
    In 1984 Blalock and Smith focused attention on certain complementary hydropathic relationships between amino acids based on the genetic code. Amino acids specified on one strand of DNA were found to be hydropathically complementary to those encoded by the opposite strand of the DNA in the same reading frame. This is so because the hydropathic character of an amino acid is determined by the second base of the triplet codon (A for hydrophilic and U for hydrophobic) with the identity of the amino acid determined by the first two bases. Consequently, peptide sequences derived from the noncoding strand of DNA, or RNA that is ...
    View more >
    In 1984 Blalock and Smith focused attention on certain complementary hydropathic relationships between amino acids based on the genetic code. Amino acids specified on one strand of DNA were found to be hydropathically complementary to those encoded by the opposite strand of the DNA in the same reading frame. This is so because the hydropathic character of an amino acid is determined by the second base of the triplet codon (A for hydrophilic and U for hydrophobic) with the identity of the amino acid determined by the first two bases. Consequently, peptide sequences derived from the noncoding strand of DNA, or RNA that is complementary to mRNA, will have an inverted pattern of hydropathy relative to the pattern of amino acids derived from the coding nucleic acid strand. These complementary peptides have been found more often than not to specifically bind to the partner peptide specified by the coding strand. This is the basis of the molecular recognition theory (MRT), as proposed by Blalock (see Blalock 1995) which hypothesizes “that complementary nucleotide sequences specify peptides or proteins that interact through complementary shapes or structures resulting from their inverted periodicity of hydrophobic and hydrophilic amino acids”.
    View less >
    Book Title
    Results & Problems in Cell Differentiation. 32: Molecular Interactions of Actin
    Volume
    32
    Publisher URI
    http://dx.doi.org/10.1007/978-3-540-46560-7
    DOI
    https://doi.org/10.1007/978-3-540-46560-7_11
    Subject
    PRE2009-Enzymes
    Publication URI
    http://hdl.handle.net/10072/64788
    Collection
    • Book chapters

    Footer

    Disclaimer

    • Privacy policy
    • Copyright matters
    • CRICOS Provider - 00233E

    Tagline

    • Gold Coast
    • Logan
    • Brisbane - Queensland, Australia
    First Peoples of Australia
    • Aboriginal
    • Torres Strait Islander