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Related Concept Videos

NMR Spectroscopy: Spin–Spin Coupling01:08

NMR Spectroscopy: Spin–Spin Coupling

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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...
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Structures of Solids02:22

Structures of Solids

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Solids in which the atoms, ions, or molecules are arranged in a definite repeating pattern are known as crystalline solids. Metals and ionic compounds typically form ordered, crystalline solids. A crystalline solid has a precise melting temperature because each atom or molecule of the same type is held in place with the same forces or energy. Amorphous solids or non-crystalline solids (or, sometimes, glasses) which lack an ordered internal structure and are randomly arranged. Substances that...
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NMR Spectroscopy Of Amines01:19

NMR Spectroscopy Of Amines

11.0K
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...
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NMR Spectroscopy of Aromatic Compounds01:14

NMR Spectroscopy of Aromatic Compounds

6.2K
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.
6.2K
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
Protein and Protein Structure02:15

Protein and Protein Structure

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Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
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Study of Protein Dynamics via Neutron Spin Echo Spectroscopy
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Protein structure determination from 13C spin-diffusion solid-state NMR spectroscopy.

Theofanis Manolikas1, Torsten Herrmann, Beat H Meier

  • 1Physical Chemistry, ETH Zurich, CH-8093 Zurich, Switzerland.

Journal of the American Chemical Society
|March 7, 2008
PubMed
Summary
This summary is machine-generated.

Proton-driven 13C spin diffusion (PDSD) NMR determines protein structures with atomic resolution. This robust method uses internuclear distance information from cross-peak intensities in microcrystalline samples.

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Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
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Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
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Area of Science:

  • Biophysical Chemistry
  • Structural Biology
  • Nuclear Magnetic Resonance Spectroscopy

Background:

  • Proton-driven 13C spin diffusion (PDSD) is a 2D NMR technique.
  • PDSD yields high signal-to-noise spectra with internuclear distance information.

Purpose of the Study:

  • To demonstrate atomic-resolution protein structure determination using PDSD.
  • To investigate the relationship between cross-peak intensities and internuclear distances.

Main Methods:

  • Utilized a uniformly 13C, 15N-labeled microcrystalline protein sample (ubiquitin).
  • Employed manual structure determination, followed by automated optimization.
  • Applied a fully automated structure determination approach.

Main Results:

  • Achieved atomic-resolution structure determination of ubiquitin.
  • Showcased the sufficiency of PDSD information content for structural analysis.
  • Investigated the correlation between spectral cross-peak intensities and internuclear distances.

Conclusions:

  • PDSD is a powerful and versatile NMR experiment for protein structure elucidation.
  • The method enables structure determination from a single microcrystalline sample.
  • Further understanding of distance-intensity correlations can refine structural analysis.