n→π* interactions in proteins

G.J Bartlett, A Choudhary,,, R.T Raines, D.N Woolfson

Research output: Contribution to journalArticle (Academic Journal)peer-review

253 Citations (Scopus)

Abstract

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 contributionn→π* interactions in proteins
Original languageEnglish
Pages (from-to)615 - 620
Number of pages6
JournalNature Chemical Biology
Volume6
DOIs
Publication statusPublished - Jul 2010

Fingerprint

Dive into the research topics of '<i>n</i>→π* interactions in proteins'. Together they form a unique fingerprint.

Cite this