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Related Concept Videos

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

¹H NMR of Conformationally Flexible Molecules: Temporal Resolution

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...
Two-Dimensional (2D) NMR: Overview01:12

Two-Dimensional (2D) NMR: Overview

The 1D NMR spectrum of large and complex molecules like natural products has complicated splitting patterns and overlapping signals, which can be easily interpreted using 2-dimensional (2D) NMR. Unlike 1D NMR, 2D NMR has two frequency axes that provide the coupling information between the nucleus A and nucleus B in a molecule. The process from which 2D spectra are obtained has four steps.
The first step is the preparation period, during which nucleus A is excited with a radiofrequency pulse.
NMR Spectrometers: Resolution and Error Correction01:14

NMR Spectrometers: Resolution and Error Correction

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

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

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.
NMR Spectrometers: Radiofrequency Pulses and Pulse Sequences01:17

NMR Spectrometers: Radiofrequency Pulses and Pulse Sequences

A pulse is a short burst of radio waves distributed over a range of frequencies that simultaneously excites all the nuclei in the sample. Upon passing a radio frequency pulse along the x-axis, the nuclei absorb energy corresponding to their Larmor frequencies and achieve resonance. This shifts the net magnetization vector from the z-axis toward the transverse plane. This angle of rotation of the magnetization vector, or the flip angle, is proportional to the duration and intensity of the pulse.
Double Resonance Techniques: Overview01:12

Double Resonance Techniques: Overview

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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Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
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Bilayer sample for fast or slow magic angle oriented sample spinning solid-state NMR spectroscopy.

Christina Sizun1, Burkhard Bechinger

  • 1Max-Planck-Institut für Biochemie, Am Klopferspitz 18A, 82152 Martinsried, Germany.

Journal of the American Chemical Society
|February 14, 2002
PubMed
Summary
This summary is machine-generated.

A new Magic Angle Oriented Spinning Spectroscopy setup improves lipid bilayer analysis. This method uses spiral-wrapped polymer films for narrower line widths and higher spinning speeds, enhancing Nuclear Magnetic Resonance (NMR) capabilities.

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Area of Science:

  • Solid-state Nuclear Magnetic Resonance (NMR) Spectroscopy
  • Biophysical Chemistry
  • Materials Science

Background:

  • Magic Angle Oriented Spinning Spectroscopy (MAOSS) is crucial for studying molecular orientation in solid-state samples.
  • Conventional MAOSS setups using stacked glass plates have limitations in spinning speed and line width.
  • Orienting lipid bilayers is essential for understanding membrane protein structure and function.

Purpose of the Study:

  • To propose and evaluate an alternative setup for Magic Angle Oriented Spinning Spectroscopy (MAOSS).
  • To improve spectral resolution and increase the accessible spinning frequency range for oriented lipid bilayer samples.
  • To enable advanced high-resolution multidimensional NMR experiments on oriented biological membranes.

Main Methods:

  • Lipid bilayers were oriented onto polymer films.
  • The polymer films with oriented bilayers were wrapped into a spiral configuration.
  • This spiral sample geometry was adapted to fit standard 4 or 7 mm MAS rotors.
  • Spectroscopic analysis was performed at various spinning frequencies.

Main Results:

  • The proposed spiral geometry resulted in significantly narrower line widths compared to conventional MAOSS setups.
  • A higher upper spinning limit was achieved with the new setup.
  • Orientational information was successfully extracted from low-spinning spectra.
  • The findings indicate suitability for high-resolution multidimensional NMR pulse sequences at fast spinning speeds.

Conclusions:

  • The alternative MAOSS setup offers superior performance for oriented lipid bilayer samples.
  • This novel geometry overcomes limitations of traditional methods, enabling enhanced NMR investigations.
  • The improved spectral quality and higher spinning capabilities open new avenues for studying complex biological systems using solid-state NMR.