Trends in Biotechnology
Volume 7, Issue 12, December 1989, Pages 354-359
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Review
Electrostatic interactions in aromatic oligopeptides contribute to protein stability

https://doi.org/10.1016/0167-7799(89)90036-XGet rights and content

Abstract

Recent X-ray crystallographic studies of aromatic oligopeptides have shown that aromatic amino acid side chains participate in enthalpically-favorable, weakly polar interactions that stabilize oligopeptide folds. These interactions are important in peptides used as model therapeutic agents for sickle-cell disease, in vasopressin (antidiuretic hormone) and in [Leu]-enkephalin. The aromatic groups of globular proteins display similar behavior and thereby contribute to the stability of the three-dimensional structure of proteins.

References (31)

  • D.J. Barlow et al.

    J. Mol. Biol.

    (1983)
  • E.N. Baker et al.

    Prog. Biophys. Mol. Biol.

    (1984)
  • S.K. Burley et al.

    Adv. Prot. Chem.

    (1988)
  • B.H. Arison et al.

    Biochem. Biophys. Res. Comm.

    (1981)
  • J. Singh et al.

    FEBS Lett.

    (1985)
  • R.H. Kretsinger et al.

    J. Biol. Chem.

    (1973)
  • K.S.C. Reid et al.

    FEBS Lett.

    (1985)
  • S.K. Burley et al.

    FEBS Lett.

    (1986)
  • M. Levitt et al.

    J. Mol. Biol.

    (1988)
  • F. London

    Trans. Faraday Soc.

    (1937)
  • S. Lifson et al.

    J. Amer. Chem. Soc.

    (1979)
  • E.G. Cox et al.
  • A.H. Narten

    J. Chem. Phys.

    (1968)
  • K.C. Janda et al.

    J. Chem. Phys.

    (1975)
  • G. Karlström et al.

    J. Amer. Chem. Soc.

    (1983)
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