Interactions between NH moiety and aromatic side chains of amino acid residues, the so-called N-H...π interaction, are supposed to contribute to the overall stability of the folded structure of peptides and proteins. The present study details the results of N-H...π interactions in relation to other factors like secondary structural elements, solvent accessibility, conservation score and stabilization centers in 'all-alpha' proteins. We observed 160 N-H....π interactions in a data set of 75 'all-alpha' proteins. Side-chain to side-chain N-H....π interactions are the predominant type of interactions in the data set. Among the various types of folds of 'all-alpha' proteins considered for the analysis, proteins belonging to alpha-alpha superhelix fold have the highest percentage of N-H...π interactions. The secondary structure preference, solvent accessibility and stabilization centers of N-H....π interacting residues were estimated. These interactions are mainly formed by long range contacts. More than 50% of the N-H....π interacting residues are highly conserved. It is likely that the N-H....π interactions contribute significantly to the overall stability of 'all-alpha' proteins.