Abstract
In this work, the role of cation-pi and CH...pi interactions in the activity of glutaredoxins is analysed. Among the proteins, an average of 1 cation-pi interaction per 109 residues and an average of 1 CH...pi interaction per 16 residues were found. These interactions were influenced by long-range contacts whereas short- and medium-range contacts were found insignificant. Significant differences in these interactions were noticed when the same glutaredoxin was analysed in its glutathionylated, reduced and oxidised states. Since activities of glutaredoxins depend on its state, the role of these interactions in regulation of these proteins might be significant.
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