From the dawn of knowledge about chemical structures in the early 1800's, through the early 1900s revealing the atomic structure, elucidation of the polymer structure in the 1920s, perception of the first protein structure about 53 years ago, to the resolution of the gene structure more recently in the 1970s, structural knowledge has always led the way for major revolutions in the chemical, physical and biological sciences over the past two centuries. The new millenium has brought with it computational proteomics, which promises a high impact revolution in our understanding of the proteome as we know it. The overall stability of the folded structure of peptides and proteins depends on the various interactions that its amino acid residues take part in. Of the various types of stabilizing interactions, in the current study we have analyzed N-H....π interactions in a set of 100 different transmembrane proteins. The present study details the results of N-H...π interactions in relation to other factors like secondary structural elements, conservation score and stabilization centers in transmembrane proteins. The obtained results suggests that the N-H....π interactions contribute significantly to the overall stability of transmembrane proteins.