Cation-π interactions are known to be important contributors to protein stability and ligand-protein interactions. In this study, we have analyzed the influence of cation-π interactions in single chain 'all-alpha' proteins. We observed 135 cation-π interactions in a data set of 75 proteins. No significant correlation was observed between the total number of amino acid residues and number of cation-π interactions. These interactions are mainly formed by long-range contacts and there is preference of Arg over Lys in these interactions. Arg-Phe interactions are predominant among the various pairs analyzed. Despite the scarcity of interactions involving Trp, the average energy for Trp-cation interactions, was quite high. This information implies that the cation-π interactions involving Trp, maybe of high relevance to the proteins. Secondary structure analysis reveals that cation-π interactions are formed preferrably between residues, in which at least one of them, is in the secondary structure of alpha-helical segments. Among the various types of folds of 'all-alpha' proteins considered for the analysis, proteins belonging to alpha-alpha superhelix fold have the highest number of cation-π interaction forming residues.
All Science Journal Classification (ASJC) codes
- Agricultural and Biological Sciences(all)