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Related Concept Videos

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

¹H NMR of Conformationally Flexible Molecules: Temporal Resolution

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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

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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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In an NMR sample, precise measurement of the absolute absorption frequencies of nuclei is difficult. A standard internal reference compound is added, and the frequency difference between the reference signal and sample signals is measured.
The internal reference compound generally used in NMR spectroscopy is tetramethylsilane (TMS). TMS is preferred because it is chemically inert, soluble in NMR solvents, and easily removable. Also, the highly shielded methyl protons in TMS yield an intense...
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Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins
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Protein Structural Ensembles Visualized by Solvent Paramagnetic Relaxation Enhancement.

Zhou Gong1, Xin-Hua Gu1, Da-Chuan Guo1

  • 1CAS Key Laboratory of Magnetic Resonance in Biological Systems, State Key Laboratory of Magnetic Resonance and Atomic Molecular Physics, National Center for Magnetic Resonance in Wuhan, Collaborative Innovation Center of Chemistry for Life Sciences, Wuhan Institute of Physics and Mathematics of the Chinese Academy of Sciences, Wuhan, Hubei Province, 430071, China.

Angewandte Chemie (International Ed. in English)
|December 20, 2016
PubMed
Summary

This study introduces a new method using solvent paramagnetic relaxation enhancement (sPRE) to measure protein dynamics and uncover alternative protein conformations. This technique enhances the understanding of protein structural ensembles and dynamics.

Keywords:
NMR spectroscopyparamagnetic relaxation enhancementsprotein dynamicsprotein structuresstructural ensembles

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Biophysics

Background:

  • Proteins exist in multiple conformations to perform their functions, but characterizing these structural ensembles is challenging.
  • Established Nuclear Magnetic Resonance (NMR) techniques like paramagnetic relaxation enhancement (PRE) are valuable but often limited to rigid protein structures.

Purpose of the Study:

  • To develop and validate a method for characterizing protein dynamics on the microsecond-millisecond timescale.
  • To expand the application of PRE NMR to study flexible proteins and identify alternative conformations.

Main Methods:

  • Accurate measurement of solvent paramagnetic relaxation enhancement (sPRE) in the presence of an inert paramagnetic cosolute.
  • Analysis of sPRE data to assess protein dynamics and structural ensembles.
  • Integration with molecular dynamics simulations to identify and validate alternative protein conformations.

Main Results:

  • The developed sPRE method successfully characterizes microsecond-millisecond dynamics in multi-domain proteins.
  • The analysis of sPRE data reveals ensembles of structures that accurately explain experimental observations.
  • The method identified previously theorized alternative protein conformations when combined with molecular dynamics simulations.

Conclusions:

  • The novel sPRE-based method expands the utility of PRE NMR beyond rigid proteins.
  • This approach provides a powerful tool for investigating protein dynamics and conformational heterogeneity.
  • The findings offer new insights into the functional relevance of protein structural ensembles.