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

作者信息

Louro Ricardo O, Catarino Teresa, Paquete Catarina M, Turner David L

机构信息

Instituto de Tecnologia Quìmica e Biológica da Universidade Nova de Lisboa, Rua da Quínta Grande 6, Apt 127, 2780-156 Oeiras, Portugal.

出版信息

FEBS Lett. 2004 Oct 8;576(1-2):77-80. doi: 10.1016/j.febslet.2004.08.066.

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 angstroms, can be described by a simple function derived from the Debye-Huckel 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.

摘要

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