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Videos de Conceptos Relacionados

¹H NMR of Labile Protons: Deuterium (²H) Substitution00:48

¹H NMR of Labile Protons: Deuterium (²H) Substitution

This lesson illustrates the role of deuterium substitution in simplifying the NMR spectrum of compounds comprising labile protons. One method employed is the use of deuterium. Amongst the three isotopes of hydrogen, deuterium (2H) has a nucleus composed of one proton and one neutron. When the D2O solvent is added to a pure dry ethanol solution, its labile proton is substituted with deuterium.
¹³C NMR: Distortionless Enhancement by Polarization Transfer (DEPT)01:20

¹³C NMR: Distortionless Enhancement by Polarization Transfer (DEPT)

When proton-coupled carbon-13 spectra are simplified by a broadband proton decoupling technique, structural information about the coupled protons is lost. Distortionless enhancement by polarization transfer (DEPT) is a technique that provides information on the number of hydrogens attached to each carbon in a molecule. While the DEPT experiment utilizes complex pulse sequences, the pulse delay and flip angle are specifically manipulated. The resulting signals have different phases depending on...
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.
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.
Applications Of NMR In Biology01:25

Applications Of NMR In Biology

Nuclear magnetic resonance (NMR) spectroscopy is a very valuable analytical technique for researchers. It has been used for more than 50 years as an analytical tool. F. Bloch and E. Purcell formulated NMR in 1946 and won the 1952 Nobel Prize in Physics  for their work. Biological macromolecules such as proteins, nucleic acids, lipids, and organic molecules including pharmaceutical compounds, can be studied using this versatile tool that exploits the magnetic properties of certain nuclei.
The...
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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Video Experimental Relacionado

Updated: Jul 16, 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

Técnicas de RMN de solución para estructuras moleculares y supramoleculares grandes.

Roland Riek1, Jocelyne Fiaux, Eric B Bertelsen

  • 1Institut für Molekularbiologie und Biophysik, Eidgenössische Technische Hochschule Zürich, CH-8093 Zürich, Switzerland.

Journal of the American Chemical Society
|October 10, 2002
PubMed
Resumen

Este estudio combina la espectroscopia optimizada para relajación transversal (TROSY) con técnicas de transferencia de polarización para analizar biomoléculas grandes utilizando RMN 2D. Los parámetros experimentales optimizados permiten espectros de alta resolución para macromoléculas de hasta 800 kDa.

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Last Updated: Jul 16, 2026

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Área de la Ciencia:

  • Química biofísica y bioquímica.
  • Biología Estructural Biología Estructural
  • Espectroscopia de Resonancia Magnética Nuclear (RMN) Espectroscopia de Resonancia Magnética Nuclear (RMN) Espectroscopia de Resonancia Magnética Nuclear (RMN) Espectroscopia de Resonancia Magnética Nuclear (RMN) Espectroscopia de Resonancia Magnética Nuclear (RMN) Espectroscopia de Resonancia Magnética Nuclear (RMN) Espectroscopia de Resonancia Magnética Nuclear (RMN) Espectroscopia de Resonancia Magnética Nuclear (RMN) Espectroscopia de Resonancia Magnética Nuclear (RMN) Espectroscopia de Resonancia Magnética Nuclear (RMN) Espectroscopia de Resonancia Magnética Nuclear (RMN) Espectroscopia de Resonancia Magnética Nuclear (RMN)

Sus antecedentes:

  • El análisis de grandes macromoléculas homooligoméricas (110-800 kDa) utilizando RMN en solución presenta desafíos debido a la ampliación de la señal.
  • Las técnicas estándar de RMN a menudo tienen dificultades para proporcionar espectros de alta resolución para estructuras biológicas tan grandes.

Objetivo del estudio:

  • Desarrollar y optimizar métodos de RMN 2D para obtener espectros de correlación de alta calidad de grandes macromoléculas homooligoméricas etiquetadas con (15) N, ((2) H.
  • Investigar el rendimiento de las técnicas TROSY combinadas con CRIPT/CRINEPT para estructuras biomoleculares grandes.

Principales métodos:

  • Espectroscopia transversal optimizada por relajación combinada (TROSY) con transferencia de polarización inducida por relajación correlacionada cruzada (CRIPT) o transferencia de polarización mejorada por relajación correlacionada cruzada (CRINEPT).
  • Los espectros de correlación de RMN de la solución 2D adquiridos de las macromoléculas homooligoméricas etiquetadas con (15) N, ((2) H que van desde 110 hasta 800 kDa.
  • Tiempos de transferencia de polarización optimizados sistemáticamente, retrasos de relajación y rutinas de manejo de agua.

Principales resultados:

  • Se obtienen espectros basados en TROSY con anchos de línea manejables (por ejemplo, ~75 Hz para 15N a 800 kDa).
  • Tiempos de transferencia de polarización óptimos determinados que son inversamente proporcionales al tamaño molecular (por ejemplo, 1,4 ms para 800 kDa).
  • Tiempos de reciclaje establecidos cortos (< 1 s) debido a la rápida relajación longitudinal de protones en H2O.

Conclusiones:

  • El enfoque combinado CRIPT/CRINEPT-TROSY efectivamente produce espectros de RMN 2D de alta resolución para las grandes macromoléculas homooligoméricas.
  • La optimización de los parámetros experimentales, particularmente los tiempos de transferencia y la supresión de agua, es crucial para el análisis exitoso de RMN de estructuras grandes.
  • Los métodos desarrollados avanzan significativamente en el estudio de RMN de grandes ensamblajes biomoleculares en solución.