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Related Concept Videos

¹H NMR of Conformationally Flexible Molecules: Temporal Resolution00:52

¹H NMR of Conformationally Flexible Molecules: Temporal Resolution

1.0K
At room temperature, the chair conformer of cyclohexane undergoes rapid ring flipping between two equivalent chair conformers at a rate of approximately 105 times per second. These two chair conformers are in equilibrium. The rapid ring flipping results in the interconversion of the axial proton to an equatorial proton and an equatorial to the axial proton. Such interconversions are too rapid and cannot be detected on the NMR timescale. Hence, the NMR spectrometer cannot distinguish between the...
1.0K
NMR Spectroscopy: Spin–Spin Coupling01:08

NMR Spectroscopy: Spin–Spin Coupling

2.5K
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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¹H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR01:15

¹H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR

1.3K
The axial and equatorial protons in cyclohexane can be distinguished by performing a variable-temperature NMR experiment. In this process, except for one proton, the remaining eleven protons are replaced by deuterium. The deuterium substitution avoids the possible peak splitting caused by the spin-spin coupling between the adjacent protons. The remaining proton flips between the axial and equatorial positions.
1.3K

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Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments
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Protein structural dynamics by Magic-Angle Spinning NMR.

Marta Bonaccorsi1, Tanguy Le Marchand1, Guido Pintacuda1

  • 1Université de Lyon, Centre de RMN à Très hauts Champs, UMR 5280 (CNRS / Ecole Normale Supérieure de Lyon / Université Claude Bernard Lyon 1), 5 rue de la Doua, F-69100, Villeurbanne, France.

Current Opinion in Structural Biology
|April 29, 2021
PubMed
Summary
This summary is machine-generated.

Magic-Angle Spinning Nuclear Magnetic Resonance (MAS NMR) is a powerful technique for characterizing protein structures and dynamics. Recent advancements enable its application to challenging protein samples, offering unique insights into conformational changes.

Keywords:
DynamicsFibrilsMagic-angle spinning NMRMembrane proteinsMicrocrystalsProteinProtein assemblies

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Area of Science:

  • Biophysics
  • Structural Biology
  • Biochemistry

Background:

  • Magic-Angle Spinning Nuclear Magnetic Resonance (MAS NMR) is a versatile technique for analyzing challenging protein samples.
  • It complements other methods like X-ray crystallography and electron microscopy.
  • MAS NMR is particularly useful for microcrystalline, poorly crystalline, or disordered protein systems.

Purpose of the Study:

  • To review recent advancements in biomolecular MAS NMR.
  • To highlight the application of MAS NMR in studying protein dynamics.
  • To showcase the growing utility of MAS NMR in structural biology.

Main Methods:

  • Magic-Angle Spinning Nuclear Magnetic Resonance (MAS NMR) spectroscopy.
  • Analysis of protein structure and dynamics.
  • Characterization of disordered and membrane-embedded systems.

Main Results:

  • MAS NMR provides unique insights into both static and dynamic disorder in proteins.
  • The technique can characterize amplitudes and timescales of molecular motion.
  • Recent studies demonstrate successful applications in diverse biological systems.

Conclusions:

  • MAS NMR is a rapidly evolving technique with significant potential in structural biology.
  • It offers complementary information to established structural methods.
  • The technique is increasingly applied to understand complex protein conformational dynamics.