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Related Concept Videos

NMR Spectrometers: Resolution and Error Correction01:14

NMR Spectrometers: Resolution and Error Correction

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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...
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Double Resonance Techniques: Overview01:12

Double Resonance Techniques: Overview

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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.
Spin decoupling is usually achieved by...
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¹H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR01:15

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

1.1K
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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Chemical Shift: Internal References and Solvent Effects01:17

Chemical Shift: Internal References and Solvent Effects

656
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...
656
¹H NMR of Conformationally Flexible Molecules: Temporal Resolution00:52

¹H NMR of Conformationally Flexible Molecules: Temporal Resolution

868
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...
868
2D NMR: Overview of Homonuclear Correlation Techniques01:16

2D NMR: Overview of Homonuclear Correlation Techniques

211
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...
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Updated: Jul 13, 2025

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Resolution in cryogenic solid state NMR: Challenges and solutions.

Ivan V Sergeyev1, Keith Fritzsching1, Rivkah Rogawski1

  • 1Columbia University, Department of Chemistry, New York, New York, USA.

Protein Science : a Publication of the Protein Society
|October 17, 2023
PubMed
Summary
This summary is machine-generated.

Cryogenic temperature Nuclear Magnetic Resonance (NMR) offers detailed biopolymer insights. Understanding spectral line broadening at low temperatures reveals conformational ensembles crucial for biological function.

Keywords:
DNPcryogenic NMRdynamic nuclear polarizationmagnetic resonanceprotein dynamicssolid state NMR

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Area of Science:

  • Biophysics
  • Structural Biology
  • Biochemistry

Background:

  • Nuclear Magnetic Resonance (NMR) spectroscopy at cryogenic temperatures presents opportunities for detailed biopolymer analysis.
  • Challenges in low-temperature NMR include broad spectral lines, which can obscure fine details.
  • Understanding the origins of this line broadening is key to unlocking the technique's full potential.

Purpose of the Study:

  • To explore hypotheses explaining line broadening in cryogenic temperature NMR spectra.
  • To investigate the role of conformational dynamics in spectral line broadening.
  • To leverage low-temperature NMR data to understand conformational ensembles driving biological function.

Main Methods:

  • Analysis of Nuclear Magnetic Resonance (NMR) spectra obtained at cryogenic temperatures.
  • Exploration of various hypotheses for spectral line broadening.
  • Investigation of conformational distributions and their temperature dependence.

Main Results:

  • Hypotheses regarding the origins of line broadening were explored.
  • Inhomogeneous conformational distributions are a significant factor, particularly when molecular motions slow down at low temperatures.
  • Low-temperature spectra reveal information about conformational ensembles.

Conclusions:

  • Cryogenic temperature NMR is a powerful tool for site-specific biopolymer characterization.
  • Line broadening in low-temperature NMR is linked to conformational heterogeneity.
  • This technique allows for the study of conformational ensembles critical to biological processes.