Enzymes are central in nearly all biological pathways and allow for more effective rate enhancement than any manmade catalysts. Therefore, gaining an understanding of enzyme mechanism has been a central goal in much of chemical research. This study develops a methodology for the use of bond dipole moment calculations for the study of local electronic structure dynamics, which are key in enzyme function and folding processes. This methodology was applied to the molecular dynamics simulations of seven model tripeptides, selected as modifications of tri-alanine to sample a range of residue types and interactions. Combined with mutual information and cross-correlation, bond dipole moments provide insight on electronic structure properties such as charge transfer and fluctuations, allowing for the characterization of conformations and residue interactions. Such observations can give rise to the improvement of force field treatments and development of systematic QM/MM methodologies. Additionally, bond dipole moments coupled with enzyme-induced electric field calculations may be used to track the stabilization and destabilization of bonds in reactions from various biological contexts, such as MTases.

Revealing electronic structure dynamics in tripeptides with bond dipole moments

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

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