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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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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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A proton M that is coupled to a proton X results in doublet signals for M. However, NMR-active nuclei can be simultaneously coupled to more than one nonequivalent nucleus. When M is coupled to a second proton A, such as in styrene oxide, each peak in the doublet is split into another doublet.
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Double resonance techniques in Nuclear Magnetic Resonance (NMR) spectroscopy involve the simultaneous application of two different frequencies or radiofrequency pulses to manipulate and observe two distinct nuclear spins. One important application of double resonance is spin decoupling, which selectively suppresses coupling with one type of nucleus while observing the NMR signal from another nucleus, simplifying the spectrum and enhancing resolution.
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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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5D solid-state NMR spectroscopy for facilitated resonance assignment.

Alexander Klein1, Suresh K Vasa1, Rasmus Linser2

  • 1Department of Chemistry and Chemical Biology, TU Dortmund University, Otto-Hahn-Str. 4a, 44227, Dortmund, Germany.

Journal of Biomolecular NMR
|November 9, 2023
PubMed
Summary
This summary is machine-generated.

Five-dimensional (5D) solid-state NMR spectroscopy streamlines protein resonance assignment. This technique enhances efficiency and accuracy for both large and small protein targets, overcoming limitations of traditional methods.

Keywords:
5DFast magic-angle spinningHigher dimensionalityMinimal set of experimentsNon-uniform samplingProton detectionResonance assignmentSolid-state NMR

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Area of Science:

  • Structural Biology
  • Biophysical Chemistry
  • Nuclear Magnetic Resonance (NMR) Spectroscopy

Background:

  • Solid-state NMR spectroscopy is vital for protein characterization.
  • Higher-dimensionality NMR aids resonance assignments in large proteins.
  • Resonance assignment is a time-limiting bottleneck in solid-state NMR.

Purpose of the Study:

  • To demonstrate 5D solid-state NMR for streamlining resonance assignment in proteins.
  • To show the applicability of 5D NMR for small to medium-sized protein targets.
  • To present 5D NMR as a practical and efficient alternative to traditional assignment methods.

Main Methods:

  • Utilized 5D solid-state NMR spectroscopy.
  • Employed non-uniform sampling and spectral reconstruction algorithms.
  • Applied to deuterated and proton back-exchanged micro-crystalline proteins at fast magic-angle spinning.

Main Results:

  • Achieved direct amide-to-amide correlations in 5D with high sensitivity.
  • Demonstrated efficient and high-confidence backbone walks for assignment.
  • Integrated sidechain-to-backbone correlations for simultaneous assignment.

Conclusions:

  • 5D solid-state NMR is effective for high-molecular-weight and smaller proteins.
  • This method offers a potent alternative to 3D assignment strategies, reducing ambiguity.
  • The approach facilitates automation and broadens access to NMR-based protein characterization.