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Related Concept Videos

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

¹H NMR of Conformationally Flexible Molecules: Temporal Resolution

888
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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¹H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR01:15

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

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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.
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Updated: Jul 27, 2025

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ARCHE-NOAH: NMR supersequence with five different CEST experiments for studying protein conformational dynamics.

Rodrigo Cabrera Allpas1, Alexandar L Hansen2, Rafael Brüschweiler1,2,3

  • 1Department of Chemistry and Biochemistry, The Ohio State University, Columbus, Ohio 43210, USA. bruschweiler.1@osu.edu.

Physical Chemistry Chemical Physics : PCCP
|June 8, 2023
PubMed
Summary
This summary is machine-generated.

A novel Nuclear Magnetic Resonance (NMR) NOAH-supersequence enables faster study of protein dynamics. This new method combines five chemical exchange saturation transfer (CEST) experiments, significantly reducing experiment time by over four days.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Nuclear Magnetic Resonance Spectroscopy

Background:

  • Studying protein dynamics is crucial for understanding biological function.
  • Traditional methods for analyzing protein dynamics using Chemical Exchange Saturation Transfer (CEST) experiments can be time-consuming.
  • Efficient acquisition of diverse dynamic information from proteins is a persistent challenge.

Purpose of the Study:

  • To introduce a novel NMR NOAH-supersequence for comprehensive protein dynamics analysis.
  • To accelerate the data acquisition process for multiple CEST experiments.
  • To enable more efficient characterization of protein backbone and side-chain dynamics.

Main Methods:

  • Development of a new NMR NOAH-supersequence integrating five distinct CEST experiments.
  • Implementation of 15N-CEST, carbonyl-13CO-CEST, aromatic-13Car-CEST, 13Cα-CEST, and methyl-13Cmet-CEST within the supersequence.
  • Comparative analysis of data acquisition time against individual CEST experiments.

Main Results:

  • The NOAH-supersequence successfully integrates five types of CEST experiments.
  • The new sequence significantly reduces the total experimental time required.
  • Time savings of over four days per sample were achieved compared to running individual experiments.

Conclusions:

  • The presented NMR NOAH-supersequence offers a highly efficient approach for studying protein dynamics.
  • This method accelerates the acquisition of crucial data for backbone and side-chain dynamics.
  • The time-saving aspect of this technique facilitates more extensive NMR studies of proteins.