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

¹H NMR of Conformationally Flexible Molecules: Temporal Resolution

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...
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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.
2D NMR: Overview of Homonuclear Correlation Techniques01:16

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Homonuclear correlation spectroscopy (COSY) is a powerful technique used in Nuclear Magnetic Resonance (NMR) spectroscopy to study the correlations between nuclei of the same type within a molecule. It provides information about scalar couplings between adjacent nuclei, which helps determine connectivity and structural information. There are several COSY variants, each with its unique strengths and experimental parameters.
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Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
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Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Published on: September 17, 2017

Structural constraints for the Crh protein from solid-state NMR experiments.

Carole Gardiennet1, Antoine Loquet, Manuel Etzkorn

  • 1Institut de Biologie et Chimie des Protéines, UMR 5086 C.N.R.S./Université de Lyon, Lyon Cedex 07, France.

Journal of Biomolecular NMR
|March 6, 2008
PubMed
Summary
This summary is machine-generated.

Proton-detected solid-state NMR experiments successfully extracted distance constraints for the large Crh protein dimer. This method provides detailed structural and dynamic information, validating its use for complex proteins.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Nuclear Magnetic Resonance (NMR) Spectroscopy

Background:

  • Solid-state NMR is crucial for determining protein structures.
  • Proton-detected experiments offer enhanced sensitivity for complex systems.
  • Understanding protein dynamics is key to function.

Purpose of the Study:

  • To extract short, medium, and long-range distance constraints from solid-state NMR experiments.
  • To analyze the structural and dynamic information of the microcrystalline Crh protein dimer.
  • To validate proton-mediated distance measurements for large, complex proteins.

Main Methods:

  • Utilized proton-mediated, rare-spin detected correlation solid-state NMR experiments.
  • Analyzed magnetization build-up curves from cross signals in NHHC and CHHC spectra.
  • Applied these methods to the 10.4 x 2 kDa dimeric model protein Crh.

Main Results:

  • Successfully extracted short, medium, and long-range constraints covering the entire protein sequence.
  • Observed inter-monomer contacts within the domain-swapped Crh dimer.
  • Demonstrated that protein dynamics influence cross-signal intensities, with mobile regions showing fewer contacts.

Conclusions:

  • Proton-mediated distance measurements are validated for complex proteins like the Crh dimer.
  • Solid-state NMR provides detailed insights into protein structure and dynamics.
  • Magnetization transfer properties in solid protein samples are confirmed.