Isotope effects on chemical shifts in the study of hydrogen bonded biological systems

Hansen, Poul Erik

doi:10.1016/j.pnmrs.2020.08.001

Cited by 7 publications

(3 citation statements)

References 55 publications

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“…Therefore, deuterium isotope effects on chemical shifts have turned out to be a useful tool in establishing the presence and the characteristics of intramolecular hydrogen bonds [4]. Examples include the use of deuterium isotope effects on 13 C chemical shifts as well as on 15 N chemical shifts in proteins [5,6]. Such isotope effects also have advantages in studies of DNA [7,8].…”

Section: Introductionmentioning

confidence: 99%

Multiple Intramolecular Hydrogen Bonding in Large Biomolecules: DFT Calculations and Deuterium Isotope Effects on 13C Chemical Shifts as a Tool in Structural Studies

Hansen

Kamounah

2023

Chemistry

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Large biomolecules often have multiple intramolecular hydrogen bonds. In the cases where these interact, it requires special tools to disentangle the patterns. Such a tool could be deuterium isotope effects on chemical shifts. The use of theoretical calculations is an indispensable tool in such studies. The present paper illustrates how DFT calculations of chemical shifts and deuterium isotope effects on chemical shifts in combination with measurements of these effects can establish the complex intramolecular hydrogen bond patterns of rifampicin as an example) The structures were calculated using DFT theoretical calculations, performed with the Gaussian 16 software. The geometries were optimized using the B3LYP functional and the Pople basis set 6-31G(d) and the solvent (DMSO) was taken into account in the PCM approach. Besides the 6-31G(d) basis set, the 6-31 G(d,p) and the 6-3111G(d,p) basis sets were also tested. The nuclear shieldings were calculated using the GIAO approach. Deuteriation was simulated by shortening the X-H bond lengths by 0.01 Å.

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Section: Introductionmentioning

confidence: 99%

Multiple Intramolecular Hydrogen Bonding in Large Biomolecules: DFT Calculations and Deuterium Isotope Effects on 13C Chemical Shifts as a Tool in Structural Studies

Hansen

Kamounah

2023

Chemistry

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“…Nuclear magnetic resonance (NMR) is a powerful tool in studying H-bonds in biomolecules [ 2 , 6 , 22 , 23 , 24 , 25 , 26 , 27 ]. Using parameters such as chemical shifts [ 28 , 29 ], J-coupling constants [ 30 , 31 , 32 ], and H-D exchange rates [ 33 , 34 ], it is possible to study not only individual hydrogen bonds’ strengths but also their couplings. In conjunction with computational simulations, 1 H NMR can reveal the H-bonding coupling within the active site of some enzymes, such as ketosteroid isomerase and photoactive yellow protein [ 35 , 36 ].…”

Section: Introductionmentioning

confidence: 99%

“…At the so-called EX2 limit, the rate is proportional to the open conformational population. Moreover, the isotope effect generated by H/D exchange can influence the chemical shifts of nearby atoms, revealing relevant hydrogen bond information [ 28 , 33 ]. However, the β-sheet H-bond cooperativity has yet to be quantitatively characterized by systematic experimental evidence.…”

Section: Introductionmentioning

confidence: 99%

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

Chen

Wang

et al. 2022

IJMS

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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 13Cα, 13Cβ, 1Hα, 1HN, 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.

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Isotope Effects in Hydrogen Bond Research

Hansen

2022

Spectroscopy and Computation of Hydrogen‐Bonded Systems

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Isotope effects on chemical shifts in the study of hydrogen bonded biological systems

Cited by 7 publications

References 55 publications

Multiple Intramolecular Hydrogen Bonding in Large Biomolecules: DFT Calculations and Deuterium Isotope Effects on 13C Chemical Shifts as a Tool in Structural Studies

Multiple Intramolecular Hydrogen Bonding in Large Biomolecules: DFT Calculations and Deuterium Isotope Effects on 13C Chemical Shifts as a Tool in Structural Studies

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

Isotope Effects in Hydrogen Bond Research

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