Noncovalent interactions between protein and DNA building blocks play a vital role in nature, including being essential for DNA replication, transcription and repair. This presentation will outline work in my group that identifies and characterizes noncovalent interactions between DNA and proteins. A special interest has been placed on contacts between the p�systems of the aromatic amino acids (HIS, PHE, TYR, TRP) and the canonical nucleobases, which can be classified as stacking (face-to-face) and T-shaped (face-to-edge) depending on the relative monomer orientation. DNA�protein interactions involving 2'-deoxyribose, as well as amino acids with nonaromatic p�systems (Arg, Asp, Glu), have also been considered. Detailed searches of experimental crystal structures and accurate calculations reveal that these interactions are likely more abundant and stronger than initially anticipated. The changes in these interactions upon damage to DNA and the implications of these results for understanding DNA repair processes may also be discussed.

Identifying and measuring π–π interactions between DNA and proteins

245th National Meeting (2013)

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