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

2D NMR: Overview of Homonuclear Correlation Techniques

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...
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...
2D NMR: Homonuclear Correlation Spectroscopy (COSY)01:06

2D NMR: Homonuclear Correlation Spectroscopy (COSY)

Homonuclear correlation spectroscopy, or COSY, is a 2-dimensional NMR technique that provides information about coupled protons. Typically, the geminal and vicinal coupling are observed. For example, consider the COSY spectrum of ethyl acetate, where its 1D proton NMR spectrum is plotted along the vertical and horizontal axes with their corresponding chemical shift scale. Three spots on the diagonal corresponding to the three peaks in the 1D proton spectrum are called diagonal peaks. The COSY...
NMR and Mass Spectroscopy of Carboxylic Acids01:30

NMR and Mass Spectroscopy of Carboxylic Acids

In ¹H NMR spectroscopy, acidic protons (–COOH) of carboxylic acids are highly deshielded and absorb far downfield, at around 9–12 ppm. The chemical shift value depends on the concentration and solvent used.
While α protons of carboxylic acids absorb at 2–2.5 ppm, β protons absorb further upfield.
Carboxylic acids are easily identified by dissolving them in deuterium oxide, which results in a rapid exchange of the acidic protons with deuterium. This leads to the disappearance of the acidic...
Chemical Shift: Internal References and Solvent Effects01:17

Chemical Shift: Internal References and Solvent Effects

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...

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Updated: Jun 12, 2026

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

Un método de asignación de resonancia para RMN de estado sólido de muestras orientadas de proteínas.

Robert W Knox1, George J Lu, Stanley J Opella

  • 1Department of Chemistry, North Carolina State University, 2620 Yarbrough Drive, Raleigh, North Carolina 27695-8204, USA.

Journal of the American Chemical Society
|June 1, 2010
PubMed
Resumen
Este resumen es generado por máquina.

Este estudio introduce un nuevo método para la asignación de espectros de RMN de estado sólido de proteínas de membrana etiquetadas uniformemente con nitrógeno-15. La técnica confirma las asignaciones existentes y ayuda a determinar las estructuras de las proteínas sin etiquetado especializado.

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Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
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Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
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Área de la Ciencia:

  • Biología Estructural Biología estructural.
  • La biofísica es la biofísica.
  • Espectroscopia de Resonancia Magnética Nuclear (RMN) Espectroscopía de Resonancia Magnética Nuclear (RMN) Espectroscopía de Resonancia Magnética Nuclear (RMN) Espectroscopía de Resonancia Magnética Nuclear (RMN) Espectroscopía de Resonancia Magnética Nuclear (RMN) Espectroscopía de Resonancia Magnética Nuclear (RMN) Espectroscopía de Resonancia Magnética Nuclear (RMN) Espectroscopía de Resonancia Magnética Nuclear (RMN) Espectroscopía de Resonancia Magnética Nuclear (RMN) Espectroscopía de Resonancia Magnética Nuclear (RMN) Espectroscopía de Resonancia Magnética Nuclear (RMN)

Sus antecedentes:

  • La asignación de espectros de RMN de estado sólido de proteínas de membrana es crucial para la determinación de la estructura.
  • Las proteínas alineadas uniaxialmente ofrecen conocimientos únicos, pero plantean desafíos de asignación.
  • Los métodos existentes a menudo requieren muestras etiquetadas selectivamente, lo que limita su amplia aplicabilidad.

Objetivo del estudio:

  • Proponer una estrategia general de asignación secuencial para proteínas de membrana uniformemente (15) etiquetadas con N y alineadas uniaxialmente.
  • Para demostrar la eficacia del método se utilizó la proteína de capa de fagos Pf1 alineada magnéticamente.
  • Para facilitar la determinación de la estructura de las proteínas de membrana a través de RMN en estado sólido.

Principales métodos:

  • Empleando una transferencia de magnetización Hartmann-Hahn no coincidente para las correlaciones mediadas por protones entre los giros de la columna vertebral (15) N.
  • Adquisición y superposición de espectros de campos locales separados intercambiados y no intercambiados.
  • Utilizando proteínas de membrana alineadas uniaxialmente, específicamente la proteína de capa de fagos Pf1.

Principales resultados:

  • Confirmación exitosa de la mayoría de las asignaciones originales de la literatura sin requerir muestras etiquetadas selectivamente.
  • Distinguir los picos cruzados de los picos principales comparando diferentes adquisiciones espectrales.
  • Aplicabilidad demostrada a proteínas de topología arbitraria.

Conclusiones:

  • La estrategia de asignación secuencial propuesta es efectiva para las proteínas de membrana uniformemente (15) etiquetadas con N y alineadas uniaxialmente.
  • Este método simplifica la asignación espectral, reduciendo la necesidad de complejas estrategias de etiquetado.
  • La técnica es valiosa para la futura determinación de la estructura basada en RMN de estado sólido de las proteínas de membrana.