Noncovalent Carbon-Bonding Interactions in Proteins

Abstract

Carbon bonds (C-bonds) are the highly directional noncovalent interactions between carbonyl-oxygen acceptors and sp³ -hybridized-carbon σ-hole donors through n→σ* electron delocalization. We have shown the ubiquitous existence of C-bonds in proteins with the help of careful protein structure analysis and quantum calculations, and have precisely determined C-bond energies. The importance of conventional noncovalent interactions such as hydrogen bond (H-bonds) and halogen bond (X-bonds) in the structure and function of biological molecules are well established, while carbon bonds C-bonds have still to be recognized. We have shown that C-bonds are present in proteins, contribute enthalpically to the overall hydrophobic interaction and play a significant role in the photodissociation mechanism of myoglobin and the binding of nucleobases to proteins.

Keywords: ab initio calculations; carbon bonding; noncovalent interactions; proteins; tetrel bonding.