Distance dependence of interactions between charged centres in proteins with common structural features

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27 Citations (Scopus)

Abstract

Data collected for interactions among redox centres, and interactions between redox centres and acid-base residues in a family of small multihaem cytochromes are analysed. The distance dependent attenuation of the interactions between non-surface charges, for separations that range from 8 to 23 (A) over circle, can be described by a simple function derived from the DebyeHuckel formalism, fit to 9.5 and 7.6 as values for the relative dielectric constant and Debye length, respectively. However, there is considerable scatter in the data despite the structural similarities among the proteins, which is discussed in the framework of using such simple models in predicting properties of novel proteins.
Original languageEnglish
Pages (from-to)77-80
Number of pages4
JournalFEBS Letters
Volume576
Issue number1-2
DOIs
Publication statusPublished - 11 Sep 2004

Keywords

  • Electrostatic interactions
  • Redox potentials
  • Dielectric function
  • Debye-Hückel
  • Hill factor
  • Cytochromes

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