Detecting the Hydrogen Bond Cooperativity in a Protein β-Sheet by H/D Exchange.

ABSTRACT: The hydrogen bond (H-bond) cooperativity in the β-sheet of GB3 is investigated by a NMR hydrogen/deuterium (H/D) exchange method. It is shown that the weakening of one backbone N-H…O=C H-bond between two β-strands, β1 and β2, due to the exchange of NH to ND of the H-bond donor in β1, perturbs the chemical shift of ¹³C_α, ¹³C_β, ¹H_α, ¹H_N, and ¹⁵N of the H-bond acceptor and its following residue in β2. Quantum mechanical calculations suggest that the -H-bond chemical shift isotope effect is caused by the structural reorganization in response to the H-bond weakening. This structural reorganization perturbs four neighboring H-bonds, with three being weaker and one being stronger, indicating that three H-bonds are cooperative and one is anticooperative with the perturbed H-bond. The sign of the cooperativity depends on the relative position of the H-bonds. This H-bond cooperativity, which contributes to β-sheet stability overall, can be important for conformational coupling across the β-sheet.

SUBMITTER: Li J 

PROVIDER: S-EPMC9740688 | biostudies-literature | 2022 Nov

REPOSITORIES: biostudies-literature