Stability of α-Helices

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This chapter focuses on the mechanism of helix formation in an isolated peptide and the factors that determine the stability of a peptide helix. Helix propensities are considered together with N-cap and C-cap propensities, because measurement of helix propensities requires knowing values of the N-cap and C-cap propensities, and vice versa. The chapter considers side-chain interactions: these include both the interaction of a charged side chain with the helix macrodipole and specific interactions between a particular pair of side chains, such as ion pair and H-bond interactions. Measurement of these interactions is of interest for two reasons: their values are needed to relate the stability of a peptide helix to its amino acid composition and sequence; and peptide helices provide one of the best systems, and probably the most sensitive system, for quantifying the energetics of side-chain interactions. It also considers briefly the present status of the Chou-Fasman hypothesis and the relation between the mechanism of α-helix formation in peptides and proteins. It is necessary to use helix-coil transition theory to understand the populated intermediates and to analyze the energetics of helix formation. The two closely related theories of α-helix formation are the Zimm-Bragg theory and the Lifson-Roig theory.

References (113)

  • K.M. Armstrong et al.

    J. Mol. Biol.

    (1993)
  • M. Blaber et al.

    J. Mol. Biol.

    (1994)
  • E.K. Bradley et al.

    J. Mol. Biol.

    (1990)
  • D.A. Cook

    J. Mol. Biol.

    (1967)
  • R. Fairman et al.

    Biophys. Chem.

    (1990)
  • R. Fairman et al.

    J. Mol. Biol.

    (1991)
  • R.S. Hodges et al.

    J. Biol. Chem.

    (1981)
  • A. Horovitz et al.

    J. Mol. Biol.

    (1992)
  • J. Janin et al.

    J. Mol. Biol.

    (1978)
  • S. Padmanabhan et al.

    J. Mol. Biol.

    (1994)
  • J.W. Prothero

    Biophys. J.

    (1966)
  • O.B. Ptitsyn

    Mol. Biol.

    (1969)
  • H. Qian

    Biophys. J.

    (1994)
  • M. Rico et al.

    FEBS Lett.

    (1983)
  • M. Rico et al.

    Biochem. Biophys. Res. Commun.

    (1984)
  • J. Sancho et al.

    J. Mol. Biol.

    (1992)
  • L. Serrano et al.

    J. Mol. Biol.

    (1992)
  • K.H. Altmann et al.

    Biopolymers

    (1990)
  • J. Åquist et al.

    Proc. Natl. Acad. Sci. U.S.A.

    (1991)
  • K.M. Armstrong et al.

    Proc. Natl. Acad. Sci. U.S.A.

    (1993)
  • J.A. Bell et al.

    Biochemistry

    (1992)
  • A. Bierzynski et al.

    Proc. Natl. Acad. Sci. U.S.A.

    (1982)
  • M. Blaber et al.

    Science

    (1993)
  • D.E. Blagdon et al.

    Biopolymers

    (1975)
  • J.E. Brown et al.

    Biochemistry

    (1971)
  • M.D. Bruch et al.

    Proteins

    (1991)
  • A. Chakrabartty et al.
  • A. Chakrabartty et al.

    Nature (London)

    (1991)
  • A. Chakrabartty et al.

    Proc. Natl. Acad. Sci. U.S.A.

    (1993)
  • A. Chakrabartty et al.

    Biochemistry

    (1993)
  • A. Chakrabartty et al.

    Protein Sci.

    (1994)
  • M. Chorev et al.

    Biochemistry

    (1991)
  • P.Y. Chou et al.

    Biochemistry

    (1974)
  • T.P. Creamer et al.

    Proc. Natl. Acad. Sci. U.S.A.

    (1992)
  • D.R. Da vies

    J. Mol. Biol.

    (1964)
  • A.J. Doig et al.

    Biochemistry

    (1994)
  • A.M. Felix et al.

    Int. J. Peptide Protein Res.

    (1988)
  • B. Forood et al.

    Proc. Natl. Acad. Sci. U.S.A.

    (1993)
  • P.J. Gans et al.

    Biopolymers

    (1991)
  • M.R. Ghadiri et al.

    J. Am. Chem. Soc.

    (1990)
  • M.R. Ghadiri et al.

    J. Am. Chem. Soc.

    (1990)
  • M. Go et al.

    J. Chem. Phys.

    (1971)
  • E.T. Harper et al.

    Biochemistry

    (1993)
  • J. Hermans et al.

    Biochemistry

    (1992)
  • W.G.J. Hoi et al.

    Nature (London)

    (1978)
  • A. Holtzer et al.
  • F.M. Hughson et al.

    Science

    (1990)
  • F.M. Hughson et al.

    Biochemistry

    (1991)
  • B.M.P. Huyghues-Despointes et al.

    Protein Sci.

    (1993)
  • S. Ihara et al.

    Biopolymers

    (1982)
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