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Related Concept Videos

¹H NMR: Interpreting Distorted and Overlapping Signals01:02

¹H NMR: Interpreting Distorted and Overlapping Signals

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 slanted or...
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...
¹³C NMR: ¹H–¹³C Decoupling01:04

¹³C NMR: ¹H–¹³C Decoupling

The probability of having two carbon-13 atoms next to each other is negligible because of the low natural abundance of carbon-13. Consequently, peak splitting due to carbon-carbon spin-spin coupling is not observed in spectra. However, protons up to three sigma bonds away split the carbon signal according to the n+1 rule, resulting in complicated spectra.
A broadband decoupling technique is used to simplify these complex, sometimes overlapping, signals. Broadband decoupling relies on a...
Atomic Absorption Spectroscopy: Interference01:25

Atomic Absorption Spectroscopy: Interference

Interference leads to systematic error in atomic absorption (AA) measurements by enhancing or diminishing the analytical signal or the background. These interferences can be grouped into three main categories: spectral interference, chemical interference, and physical interference.
Spectral interference occurs when signals from other elements or molecules overlap with the analyte signal, falsely elevating or masking the analyte's absorbance. This interference can be corrected using Zeeman,...
Inductively Coupled Plasma-Mass Spectrometry (ICP-MS): Interferences01:20

Inductively Coupled Plasma-Mass Spectrometry (ICP-MS): Interferences

Inductively coupled plasma–mass spectrometry (ICP–MS) is a highly selective and sensitive technique for accurate elemental analysis. Though the analysis of ICP–MS mass spectra is comparatively straightforward, it is affected by spectroscopic and non-spectroscopic interferences. Spectroscopic interferences arise when the plasma contains ionic species with an m/z value the same as the analyte ion. Spectroscopic interference can be categorized as isobaric, polyatomic ions, and refractory oxide ion...
NMR Spectroscopy: Chemical Shift Overview01:15

NMR Spectroscopy: Chemical Shift Overview

The position of the absorption signal of a sample is reported relative to the position of the signal of tetramethylsilane (TMS), which is added as an internal reference while recording spectra. The difference between the absorption frequencies of the sample and TMS (in Hz) is divided by the spectrometer operating frequency (in MHz) to obtain a dimensionless quantity called the chemical shift. It is reported on the δ (delta) scale and expressed in parts per million.
For instance, the proton...

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Updated: Jul 13, 2026

High-Temperature and High-Pressure In situ Magic Angle Spinning Nuclear Magnetic Resonance Spectroscopy
08:55

High-Temperature and High-Pressure In situ Magic Angle Spinning Nuclear Magnetic Resonance Spectroscopy

Published on: October 9, 2020

Differential line broadening in MAS solid-state NMR due to dynamic interference.

Veniamin Chevelkov1, Katja Faelber, Anna Schrey

  • 1Leibniz-Forschungsinstitut für Molekulare Pharmakologie (FMP), Robert-Rössle-Str. 10, D-13125 Berlin, Germany, and Charité Universitätsmedizin, D-10115 Berlin, Germany.

Journal of the American Chemical Society
|August 1, 2007
PubMed
Summary

Nanosecond-microsecond dynamics in solid-state NMR cause 15N resonance line broadening, hindering protein analysis. Advanced techniques like Transverse Relaxation Optimized Spectroscopy (TROSY) are crucial for high-resolution spectra of biological samples.

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

Published on: September 17, 2017

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Last Updated: Jul 13, 2026

High-Temperature and High-Pressure In situ Magic Angle Spinning Nuclear Magnetic Resonance Spectroscopy
08:55

High-Temperature and High-Pressure In situ Magic Angle Spinning Nuclear Magnetic Resonance Spectroscopy

Published on: October 9, 2020

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
14:55

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

Published on: September 17, 2017

Area of Science:

  • Biophysics
  • Structural Biology
  • Nuclear Magnetic Resonance (NMR) Spectroscopy

Background:

  • Solid-state NMR is vital for studying biological proteins.
  • Poor spectral resolution, especially in the 15N dimension, limits current NMR applications.
  • Protein dynamics can significantly impact spectral quality.

Purpose of the Study:

  • To investigate the impact of nanosecond-microsecond timescale dynamics on 15N resonances in solid-state NMR.
  • To identify the cause of line broadening in 15N NMR spectra of biological samples.
  • To propose solutions for improving spectral resolution in solid-state NMR.

Main Methods:

  • Magic Angle Spinning (MAS) solid-state NMR experiments.
  • Analysis of 15N chemical shift dimension resolution.
  • Application of Transverse Relaxation Optimized Spectroscopy (TROSY) techniques.
  • Utilizing intense deuteration strategies.

Main Results:

  • Nanosecond-microsecond dynamics induce significant 15N resonance line broadening.
  • Proton decoupling in combination with N-H spin pair motion causes effective 15N coherence relaxation.
  • TROSY-type techniques successfully select narrow spectral components, improving resolution.
  • High-resolution spectra are achievable only when dynamics are absent, very fast, or managed by TROSY.

Conclusions:

  • Protein dynamics are a major impediment to high-resolution solid-state NMR of membrane proteins and fibrillar aggregates.
  • TROSY-based methods are essential for overcoming dynamic line broadening.
  • Intense deuteration combined with advanced NMR techniques will enhance the quality and speed of future solid-state NMR investigations.