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NMR Spectroscopy Of Amines01:19

NMR Spectroscopy Of Amines

11.1K
In proton NMR spectroscopy, primary amines and secondary amines showcase their N–H protons as a broad signal in the chemical shift range between δ 0.5 and 5 ppm. The exact position in this range depends on several factors, including sample concentration, hydrogen bonding, and the type of solvent used. Since amine protons undergo fast proton exchange in solution, the protons are labile and therefore do not participate in any splitting with adjacent protons. Thus, the observed peak is...
11.1K
NMR Spectroscopy of Aromatic Compounds01:14

NMR Spectroscopy of Aromatic Compounds

6.3K
Aromatic compounds can be identified or analyzed using proton NMR and carbon‐13 NMR. Typically, aromatic hydrogens or hydrogens directly bonded to the aromatic rings are strongly deshielded by the aromatic ring current. Therefore, they absorb in the range of 6.5–8.0 ppm in proton NMR spectra. For instance, aromatic hydrogens directly bonded to the benzene ring absorb at 7.3 ppm. However, aromatic hydrogens of larger rings absorb farther upfield or downfield than the ideal range.
6.3K
NMR Spectroscopy of Benzene Derivatives01:34

NMR Spectroscopy of Benzene Derivatives

11.1K
Simple unsubstituted benzene has six aromatic protons, all chemically equivalent. Therefore, benzene exhibits only a singlet peak at δ 7.3 ppm in the 1H NMR spectrum. The observed shift is far downfield because the aromatic ring current strongly deshields the protons. Any substitution on the benzene ring makes the aromatic protons nonequivalent, and the protons split each other. The peak is, therefore, no longer a singlet and the splitting pattern and their associated coupling...
11.1K
Electron Paramagnetic Resonance (EPR) Spectroscopy: Organic Radicals01:17

Electron Paramagnetic Resonance (EPR) Spectroscopy: Organic Radicals

3.4K
Ideally, an unpaired electron shows a single peak in the EPR spectrum due to the transition between the two spin energy states. However, coupling interactions can occur between the spins of the unpaired electron and any neighboring spin-active nuclei. This hyperfine coupling results in hyperfine splitting, where the EPR signal is split into multiplets. The signals split into 2nI + 1 peaks, where n is the number of equivalent nuclei and I is the nuclear spin. These splitting patterns provide...
3.4K
NMR Spectroscopy: Chemical Shift Overview01:15

NMR Spectroscopy: Chemical Shift Overview

3.3K
The position of the absorption signal of a sample is reported relative to the position of the signal of tetramethylsilane (TMS), which is added as an internal reference while recording spectra. The difference between the absorption frequencies of the sample and TMS (in Hz) is divided by the spectrometer operating frequency (in MHz) to obtain a dimensionless quantity called the chemical shift. It is reported on the δ (delta) scale and expressed in parts per million.
For instance, the proton...
3.3K
NMR Spectroscopy: Spin–Spin Coupling01:08

NMR Spectroscopy: Spin–Spin Coupling

3.2K
The spin state of an NMR-active nucleus can have a slight effect on its immediate electronic environment. This effect propagates through the intervening bonds and affects the electronic environments of NMR-active nuclei up to three bonds away; occasionally, even farther. This phenomenon is called spin–spin coupling or J-coupling. Coupling interactions are mutual and result in small changes in the absorption frequencies of both nuclei involved. While nuclei of the same element are involved...
3.2K

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Capturing a dynamically interacting inhibitor by paramagnetic NMR spectroscopy.

Pavel Srb1, Michal Svoboda, Ladislav Benda

  • 1Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Prague, Czech Republic. veverka@uochb.cas.cz.

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Summary

Characterizing weak biomolecular interactions is challenging. This study uses paramagnetic NMR and computational methods to determine the structure of dynamic protein-ligand complexes, like HIV-1 protease with a metallacarborane ligand.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Chemical Physics

Background:

  • Transient intermolecular interactions are crucial for biological processes but difficult to study.
  • Paramagnetic ligands can enhance NMR signals, aiding the characterization of weak interactions.

Purpose of the Study:

  • To develop and validate an approach for characterizing dynamic protein-ligand complexes.
  • To investigate the interaction between HIV-1 protease and a metallacarborane ligand.

Main Methods:

  • Utilizing paramagnetic Nuclear Magnetic Resonance (NMR) experiments.
  • Employing quantum chemical calculations.
  • Performing molecular dynamics simulations.
  • Generating and analyzing large ensembles of atomic models.

Main Results:

  • Standard NMR fitting of pseudocontact shifts was insufficient for structural interpretation due to data averaging.
  • The developed approach successfully predicted and averaged experimental data from an ensemble of models.
  • Structural characterization of the dynamic HIV-1 protease-ligand complex was achieved.

Conclusions:

  • A combination of paramagnetic NMR, quantum chemistry, and molecular dynamics is effective for structural characterization of dynamic protein-ligand complexes.
  • This integrated approach overcomes limitations of standard NMR methods for averaged experimental data.