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Distance dependence of interactions between charged centres in proteins with common structural features
Author(s) -
Louro Ricardo O.,
Catarino Teresa,
Paquete Catarina M.,
Turner David L.
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.08.066
Subject(s) - debye , formalism (music) , redox , debye–hückel equation , chemistry , attenuation , chemical physics , computational chemistry , physics , quantum mechanics , inorganic chemistry , art , musical , organic chemistry , electrode , electrolyte , visual arts
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 Å, can be described by a simple function derived from the Debye–Hückel 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.