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Study of ionization of tyrosine residues in proteins by second-derivative UV spectroscopy

  • Chemistry of Natural Compounds and Bioorganic Chemistry
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Russian Chemical Bulletin Aims and scope

Abstract

Four spectrally different forms of tyrosine residues were shown to be present in proteins, namely, nonionized residues, either buried or exposed to solvent, and ionized residues buried or exposed to solvent. A method for determining the pK a values of the tyrosine residues in proteins was proposed. It is based on the decrease in the absorption intensity in the second derivative of the UV spectrum at 284.2 nm, which is the wavelength of the isobestic point corresponding to the transition of the nonionized tyrosine residues from the buried to the exposed state. Several proteins were studied by this method; the results obtained were found to be close to the corresponding published data. This method is simpler than the conventional UV titration.

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Authors and Affiliations

  1. Department of Chemistry, M. V. Lomonosov Moscow State University, Vorob'evy Gory, 119899, Moscow, Russian Federation

    L. P. Breydo, A. A. Shevchenko & O. A. Kost

Authors
  1. L. P. Breydo
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  2. A. A. Shevchenko
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  3. O. A. Kost
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Translated fromIzvestiya Akademii Nauk. Seriya Khimicheskaya, No. 7, pp. 1394–1398, July, 1997.

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Breydo, L.P., Shevchenko, A.A. & Kost, O.A. Study of ionization of tyrosine residues in proteins by second-derivative UV spectroscopy. Russ Chem Bull 46, 1339–1343 (1997). https://doi.org/10.1007/BF02495938

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  • DOI: https://doi.org/10.1007/BF02495938

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