Short hydrogen bonds, which have the donor-acceptor heavy atom distances below 2.7 Å, have been associated with essential biological functions ranging from enzyme catalysis to cellular signal transduction. These biological short hydrogen bonds often exhibit elongated O–H or N–H bonds and prominently downfield (&gt; 15 ppm) 1H NMR chemical shifts. In this work, we consider a series of model molecules that mimic the short hydrogen bonds in proteins and use ab initio molecular dynamics and ab initio path integral molecular dynamics simulations to elucidate how the interplay of electronic and nuclear quantum effects promotes proton sharing and enhances the symmetry in these compact structures. We further reveal that their 1H NMR chemical shifts follow a universal trend as the protons move in the hydrogen bonds, and uncover the crucial role of quantum effects in determining the observed downfield chemical shift.

Symmetry and 1H NMR chemical shifts of short hydrogen bonds

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

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