Hydrogen exchange study of the conformational stability of human carbonic anhydrase B and its metallocomplexes

P. Závodszky, J. T. Johansen, A. Hvidt

Research output: Chapter in Book/Report/Conference proceedingChapter

34 Citations (Scopus)

Abstract

In the range of pH 4.6 to 8.8, 25°C, the apoenzyme of carbonic anhydrase B shows no evidence of any gross conformational changes, as studied by the hydrogen deuterium exchange method. At pH 4.6, the addition of Co(II), Cd(II) or Mn(II) to the apoenzyme results in a destabilization of the native protein conformation, but in the range of pH 5.5 to 8.8 these metal ions, and Zn(II), slightly increase the conformational stability of the protein, in so far as they reduce the probability of solvent exposure of the peptide groups. In comparison with other proteins studied, native carbonic anhydrase is characterized by a rather compact conformation; for half of the peptide groups the probability of solvent exposure is less than 10-4, corresponding to changes in standard free energy larger than 5.5 kcal mol-1 (23 kJ mol-1) following the conformational transitions by which these groups are exposed to the solvent.

Original languageEnglish
Title of host publicationEUR.J.BIOCHEM.
Pages67-72EJBCAGFA
Volume56
Edition1
Publication statusPublished - 1975

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Carbonic Anhydrase I
Apoenzymes
Hydrogen
Conformations
Peptides
Protein Conformation
Proteins
Carbonic Anhydrases
Protein Stability
Deuterium
Free energy
Metal ions
Metals
Ions

ASJC Scopus subject areas

  • Medicine(all)
  • Biochemistry

Cite this

Závodszky, P., Johansen, J. T., & Hvidt, A. (1975). Hydrogen exchange study of the conformational stability of human carbonic anhydrase B and its metallocomplexes. In EUR.J.BIOCHEM. (1 ed., Vol. 56, pp. 67-72EJBCAGFA)

Hydrogen exchange study of the conformational stability of human carbonic anhydrase B and its metallocomplexes. / Závodszky, P.; Johansen, J. T.; Hvidt, A.

EUR.J.BIOCHEM.. Vol. 56 1. ed. 1975. p. 67-72EJBCAGFA.

Research output: Chapter in Book/Report/Conference proceedingChapter

Závodszky, P, Johansen, JT & Hvidt, A 1975, Hydrogen exchange study of the conformational stability of human carbonic anhydrase B and its metallocomplexes. in EUR.J.BIOCHEM.. 1 edn, vol. 56, pp. 67-72EJBCAGFA.
Závodszky P, Johansen JT, Hvidt A. Hydrogen exchange study of the conformational stability of human carbonic anhydrase B and its metallocomplexes. In EUR.J.BIOCHEM.. 1 ed. Vol. 56. 1975. p. 67-72EJBCAGFA
Závodszky, P. ; Johansen, J. T. ; Hvidt, A. / Hydrogen exchange study of the conformational stability of human carbonic anhydrase B and its metallocomplexes. EUR.J.BIOCHEM.. Vol. 56 1. ed. 1975. pp. 67-72EJBCAGFA
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