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Related Concept Videos

NMR Spectrometers: Resolution and Error Correction01:14

NMR Spectrometers: Resolution and Error Correction

1.1K
When magnetic nuclei in a sample achieve resonance and undergo relaxation, the signal detected in NMR is an approximately exponential free induction decay. Fourier transform of an exponential decay yields a Lorentzian peak in the frequency domain. Lorentzian peaks in an NMR spectrum are defined by their amplitude, full width at half maximum, and position, where the peak width is governed by the spin-spin relaxation time alone. In real experiments, however, the applied magnetic field is rendered...
1.1K
¹H NMR of Conformationally Flexible Molecules: Temporal Resolution00:52

¹H NMR of Conformationally Flexible Molecules: Temporal Resolution

1.4K
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...
1.4K
¹H NMR: Interpreting Distorted and Overlapping Signals01:02

¹H NMR: Interpreting Distorted and Overlapping Signals

1.7K
Spin systems where the difference in chemical shifts of the coupled nuclei is greater than ten times J are called first-order spin systems. These nuclei are weakly coupled, and their chemical shifts and coupling constant can generally be estimated from the well-separated signals in the spectrum.
As Δν decreases and the signals move closer, the doublets appear increasingly distorted. The intensities of the inner lines increase at the cost of those of the outer lines as the signals are...
1.7K
¹H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR01:15

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

1.8K
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.
1.8K
Atomic Nuclei: Magnetic Resonance01:05

Atomic Nuclei: Magnetic Resonance

1.3K
The number of nuclear spins aligned in the lower energy state is slightly greater than those in the higher energy state. In the presence of an external magnetic field, as the spins precess at the Larmor frequency, the excess population results in a net magnetization oriented along the z axis. When a pulse or a short burst of radio waves at the Larmor frequency is applied along the x axis, the coupling of frequencies causes resonance and flips the nuclear spins of the excess population from the...
1.3K
2D NMR: Overview of Homonuclear Correlation Techniques01:16

2D NMR: Overview of Homonuclear Correlation Techniques

743
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.
COSY90 is the standard two-dimensional (2D) COSY experiment that...
743

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Related Experiment Video

Updated: Mar 6, 2026

High-Pressure NMR Experiments for Detecting Protein Low-Lying Conformational States
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High-Pressure NMR Experiments for Detecting Protein Low-Lying Conformational States

Published on: June 29, 2021

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High-resolution NMR in the native state.

Marc Baldus1

  • 1NMR Spectroscopy, Bijvoet Center for Biomolecular Research, Utrecht University , 3584 CH Utrecht, The Netherlands.

Iucrj
|March 3, 2017
PubMed
Summary
This summary is machine-generated.

High-resolution nuclear magnetic resonance (NMR) allows detailed study of biomolecular structures. Recent advancements in in-cell NMR are enabling researchers to analyze these structures within living prokaryotic and eukaryotic cells.

Keywords:
cellular environmentcellular structural biologyin-cell NMRnuclear magnetic resonanceprotein interactions

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Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
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Area of Science:

  • Biophysics
  • Structural Biology
  • Biochemistry

Background:

  • High-resolution Nuclear Magnetic Resonance (NMR) spectroscopy offers powerful capabilities for investigating biomolecular structures.
  • Studying biomolecules in their native cellular environment presents unique challenges and opportunities.

Purpose of the Study:

  • To review the progress and potential of in-cell NMR techniques.
  • To highlight the application of in-cell NMR in both prokaryotic and eukaryotic systems.

Main Methods:

  • In-cell NMR spectroscopy applied to cellular preparations.
  • Analysis of biomolecular structure and dynamics within living cells.

Main Results:

  • Demonstration of the feasibility of obtaining high-resolution NMR data from within cells.
  • Insights into biomolecular organization and function in native cellular contexts.

Conclusions:

  • In-cell NMR is a rapidly advancing field with significant potential for understanding cellular processes.
  • This technique opens new avenues for structural biology research in native biological systems.