Some Factors in the Interpretation of Protein Denaturation1

https://doi.org/10.1016/S0065-3233(08)60608-7Get rights and content

Publisher Summary

This chapter explores that the changes that take place in the protein molecules during denaturation constitute one of the most interesting and complex classes of reactions that can be found either in nature or in the laboratory. These reactions are important because of the information they can provide about the more intimate details of protein structure and function. They are also significant because they challenge the chemist with a difficult area for the application of chemical principles. The chapter reviews that the denaturation is a process in which the spatial arrangement of the polypeptide chains within the molecule is changed from that typical of the native protein to a more disordered arrangement. The chapter also discusses the classification of protein structures: primary, secondary, and tertiary structures. The primary structure is that expressed by the structural chemical formula and depends entirely on the chemical valence bonds that the classical organic chemist would write down for the protein molecule. The secondary structure is the configuration of the polypeptide chain that results from the satisfaction of the hydrogen bonding potential between the peptide N-H and C=O groups. The tertiary structure is the pattern according to which the secondary structures are packed together within the native protein molecule. The term “denaturation” as used in this chapter is indented to include changes in both the secondary and tertiary structures.

References (259)

  • C.B. Anfinsen et al.

    Biochim. et Biophys. Acta

    (1955)
  • M.L. Anson

    Advances in Protein Chem.

    (1945)
  • G.H. Beaven et al.

    Advances in Protein Chem.

    (1952)
  • A. Berger et al.

    Arch. Biochem. Biophys.

    (1957)
  • P.D. Boyer

    J. Biol. Chem.

    (1945)
  • P.D. Boyer et al.

    J. Biol. Chem.

    (1946)
  • P.D. Boyer et al.

    J. Biol. Chem.

    (1947)
  • H. Bull

    Biochim. et Biophys. Acta

    (1956)
  • H. Bull

    Arch. Biochem. Biophys.

    (1957)
  • D.F. Cheesman et al.

    Advances in Protein Chem.

    (1954)
  • E.L. Duggan et al.

    J. Biol. Chem.

    (1948)
  • M.G. Evans et al.

    Biochim. et Biophys. Acta

    (1949)
  • H.L. Frisch et al.
  • L.J. Gosting

    Advances in Protein Chem.

    (1956)
  • G.H. Haggis

    Biochim. et Biophys. Acta

    (1956)
  • G.H. Haggis

    Biochim. et Biophys. Acta

    (1957)
  • R.G. Hart

    Biochim. et Biophys. Acta

    (1956)
  • T.L. Hill

    Arch. Biochem. Biophys.

    (1955)
  • A. Hvidt

    Biochim. et Biophys. Acta

    (1955)
  • American Petroleum Institute

    “Selected Values of Physical and Thermo-dynamic Properties of Hydrocarbons and Related Compounds”

    (1953)
  • C.B. Anfinsen

    Compt. rend. trav. lab. Carlsberg. Sér. chim.

    (1956)
  • M.L. Anson
  • M.L. Anson et al.

    J. Gen. Physiol.

    (1933)
  • M.L. Anson et al.

    J. Gen. Physiol.

    (1934)
  • U.W. Arndt et al.

    Phil. Trans. Roy. Soc. London

    (1955)
  • R. Arnold et al.

    Rec. trav. chim.

    (1950)
  • W.T. Astbury

    Trans. Faraday Soc.

    (1940)
  • W.T. Astbury et al.

    Biochem. J.

    (1935)
  • M.C. Baker et al.

    J. Am. Chem. Soc.

    (1956)
  • C.H. Bamford et al.

    “Synthetic Polypeptides.”

    (1956)
  • E. Baud

    Bull. soc. chim. France

    (1915)
  • S.M. Beiser et al.

    Science

    (1959)
  • H. Benoit

    Ann. phys.

    (1951)
  • H. Benoit

    J. chim. phys.

    (1951)
  • Beychok, S., and Steinhart, J. (1959). Abstr. 136th Meeting Am. Chem. Soc. (Boston), p....
  • R.L. Bohon et al.

    J. Am. Chem. Soc.

    (1951)
  • J.A.V. Butler

    Trans. Faraday Soc.

    (1937)
  • A. Buzzell et al.

    J. Am. Chem. Soc.

    (1951)
  • A. Buzzell et al.

    J. Am. Chem. Soc.

    (1952)
  • P.A. Charlwood

    J. Am. Chem. Soc.

    (1957)
  • H. Chick et al.

    Biochem. J.

    (1913)
  • L.K. Christensen

    Compt. rend. trav. lab. Carlsberg. Sér. chim.

    (1952)
  • W.F. Claussen

    J. Chem. Phys.

    (1951)
  • W.F. Claussen et al.

    J. Am. Chem. Soc.

    (1952)
  • E.J. Cohn

    Ann. Rev. Biochem.

    (1935)
  • E.J. Cohn et al.

    “Proteins, Amino Acids and Peptides as Dipolar Ions”

    (1943)
  • L.C. Craig et al.

    J. Am. Chem. Soc.

    (1955)
  • L.C. Craig et al.

    J. Am. Chem. Soc.

    (1957)
  • F. Cramer

    “Einschlussverbindungen”

    (1954)
  • J.L. Crammer et al.

    Bihem. J.

    (1943)
  • Cited by (4173)

    View all citing articles on Scopus
    1

    The preparation of this article has been assisted by a grant from the National Science Foundation.

    View full text