Hydrogen bonds between backbone amides are common in folded proteins. Here, we show that an intimate interaction between backbone amides also arises from the delocalization of a lone pair of πelectrons (n) from an oxygen atom to the antibonding orbital (π*) of the subsequent carbonyl group. Natural bond orbital analysis predicted significant n→π* interactions in certain regions of the Ramachandran plot. These predictions were validated by a statistical analysis of a large, non-redundant subset of protein structures determined to high resolution. The correlation between these two independent studies is striking. Moreover, the n→π* interactions are abundant and especially prevalent in common secondary structures such as a-, 310- and polyproline II helices and twisted b-sheets. In addition to their evident effects on protein structure and stability, n→π* interactions could have important roles in protein folding and function, and merit inclusion in computational force fields.
|Translated title of the contribution||n→π* interactions in proteins|
|Pages (from-to)||615 - 620|
|Number of pages||6|
|Journal||Nature Chemical Biology|
|Publication status||Published - Jul 2010|