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Role of Cation-π Interactions in Single chain 'All-alpha' Proteins

Martis, Remila L and Singh, Sameer Kumar and Gromiha, Michael M and Santhosh, C (2008) Role of Cation-π Interactions in Single chain 'All-alpha' Proteins. Journal of Theoretical Biology, 250 (4). pp. 655-662.

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Abstract

Cation-pi interactions are known to be important contributors to protein stability and ligand-protein interactions. In this study, we have analyzed the influence of cation-pi interactions in single chain 'all-alpha' proteins. We observed 135 cation-pi 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-pi 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-pi interactions involving Trp, maybe of high relevance to the proteins. Secondary structure analysis reveals that cation-pi interactions are formed preferably 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-pi interaction forming residues.

Item Type: Article
Uncontrolled Keywords: Cation-piinteractions,alpha protiens,Interaction energy,Secondary structure
Subjects: Life Sciences > MLSC Manipal
Depositing User: KMC Manipal
Date Deposited: 22 Oct 2011 09:52
Last Modified: 22 Oct 2011 09:52
URI: http://eprints.manipal.edu/id/eprint/1572

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