Significance of amino acid sequence in characterization of unidentified major proteins of the organ of Corti (OC)

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  • Isolde Thalmann
    Department of Otolaryngology, Washington University, St. Louis, MO 63110
  • Ruediger Thalmann
    Department of Otolaryngology, Washington University, St. Louis, MO 63110

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<jats:p>Previously, two low molecular weight, highly acidic proteins were discribed that are present at very high concentrations in the OC and that are assigned the tentative names OCP-1 and OCP-2 [Thalmann et al., Arch. Otorhinolarygol. 226, 123–128 (1980)]. Now amino acid sequencing studies of these proteins have been initiated. Preliminary results show that the N-terminal sequence of OCP-2 is Pro-Gly-Ile-Lys-Leu-Gln-Ser-Ser-Asp-Gly-Glu-Ile-Phe-Glu-Val-Asp-X-X-Ile-Ala-Lys-Gln-. Among the advantages of knowing the sequence or primary structure are (1) the primary structure contains all the information required for formation of the secondary and tertiary structure; (2) comparison with sequences of known proteins allows determination of the degree of homology, to obtain clues about evolutionary history and degree of conservation, and hints about protein function (e.g., the “EF hand” in some calcium-binding proteins); (3) repeating motifs suggest structural role; (4) internal homology suggests duplication (e.g., in calmodulin); (5) the nature of the N-terminal residue gives clues about the turnover of the protein; and (6) the amino acid sequence allows oligopeptides to be synthesized for obtaining antibodies for immunohistochemical studies and corresponding oligonucleotides to be synthesized for molecular biologic studies. [Work supported by NIH and DRF.]</jats:p>

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