Abstract
While, intramolecular hydrogen bonds have attracted the greatest attention in studies of peptide conformations, the recognition that several other weakly polar interactions may be important determinants of folded structure has been growing. Burley and Petsko (1988) provided a comprehensive overview of the importance of weakly polar interactions, in shaping protein structures. The interactions between aromatic rings, which are spatially proximate have attracted special attention. A survey of the proximal aromatic residue pairs in proteins, allowed Burley and Petsko (1985) to suggest that, “phenyl ring centroids are separated by a preferential distance of between 4.5 and 7A, and dihedral angles approximately 90° are most common”.
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