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Videos de Conceptos Relacionados

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...
Carbon-13 (¹³C) NMR: Overview01:10

Carbon-13 (¹³C) NMR: Overview

Carbon-13 is a naturally occurring NMR-active isotope of carbon with a low natural abundance of 1.1%. In contrast, carbon-12 is the most abundant isotope of carbon with zero nuclear spin. Therefore, it is NMR inactive. The gyromagnetic ratio of carbon-13 is smaller than that of protons. As a result, carbon-13 resonance is about 6000 times weaker than proton resonance. For a given magnetic field strength, the resonance frequency of carbon-13 is about one-fourth of the resonance frequency for...
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...
NMR Spectroscopy: Spin–Spin Coupling01:08

NMR Spectroscopy: Spin–Spin Coupling

The spin state of an NMR-active nucleus can have a slight effect on its immediate electronic environment. This effect propagates through the intervening bonds and affects the electronic environments of NMR-active nuclei up to three bonds away; occasionally, even farther. This phenomenon is called spin–spin coupling or J-coupling. Coupling interactions are mutual and result in small changes in the absorption frequencies of both nuclei involved. While nuclei of the same element are involved in...
2D NMR: Overview of Heteronuclear Correlation Techniques01:18

2D NMR: Overview of Heteronuclear Correlation Techniques

Heteronuclear correlation spectroscopy is an analytical technique that investigates the coupling between different types of nuclei, often a proton and an X-nucleus, such as carbon-13 or nitrogen-15. This method is commonly used in nuclear magnetic resonance (NMR) spectroscopy to gain insights into complex chemical compounds' structural and compositional aspects. A typical heteronuclear correlation spectrum displays X-nucleus chemical shifts on one axis and a proton spectrum on the other axis.
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...

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Video Experimental Relacionado

Updated: Jun 8, 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

Interacciones supramoleculares probadas por la espectroscopia de RMN de estado sólido 13C-13C.

Antoine Loquet1, Karin Giller, Stefan Becker

  • 1Department of NMR-Based Structural Biology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany.

Journal of the American Chemical Society
|October 12, 2010
PubMed
Resumen

Desarrollamos un método de RMN de estado sólido para estudiar las interfaces de proteínas en complejos insolubles. Esta técnica reveló que las fibrillas de alfa-sinucleína asociadas a la enfermedad de Parkinson se apilan en un arreglo paralelo en el registro.

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Measuring Interactions of Globular and Filamentous Proteins by Nuclear Magnetic Resonance Spectroscopy (NMR) and Microscale Thermophoresis (MST)
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Measuring Interactions of Globular and Filamentous Proteins by Nuclear Magnetic Resonance Spectroscopy (NMR) and Microscale Thermophoresis (MST)

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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

Measuring Interactions of Globular and Filamentous Proteins by Nuclear Magnetic Resonance Spectroscopy (NMR) and Microscale Thermophoresis (MST)
10:28

Measuring Interactions of Globular and Filamentous Proteins by Nuclear Magnetic Resonance Spectroscopy (NMR) and Microscale Thermophoresis (MST)

Published on: November 2, 2018

Área de la Ciencia:

  • La bioquímica es la bioquímica.
  • Biología Estructural Biología estructural.
  • La neurociencia es la neurociencia.

Sus antecedentes:

  • Las interacciones proteína-proteína son cruciales para la función celular.
  • Los agregados de proteínas insolubles y no cristalinos, como los de las enfermedades neurodegenerativas, presentan desafíos para la determinación estructural.
  • Comprender la estructura de las fibrillas de alfa-sinucleína es clave para la investigación de la enfermedad de Parkinson.

Objetivo del estudio:

  • Desarrollar un método robusto de RMN en estado sólido para determinar las interfaces moleculares en complejos de proteínas insolubles.
  • Para dilucidar la disposición estructural de las fibrillas de alfa-sinucleína asociadas con la enfermedad de Parkinson.

Principales métodos:

  • Se utilizó la espectroscopia de resonancia magnética nuclear (RMN) de estado sólido.
  • Se midieron las distancias intermoleculares de carbono-13 (13C) carbono-13 (13C).
  • Se utilizan mezclas de proteínas etiquetadas con glucosa [1-(13) C] y glucosa [2-(13) C].

Principales resultados:

  • Determinó con éxito las interfaces moleculares en complejos proteína-proteína insolubles y no cristalinos.
  • Se estableció que las fibrillas de alfa-sinucleína están dispuestas de manera paralela en el registro.
  • Recopilación de restricciones de distancia intermolecular que permiten la determinación de la estructura de resolución atómica de las fibrillas.

Conclusiones:

  • El enfoque de RMN de estado sólido desarrollado es efectivo para caracterizar ensamblajes de proteínas difíciles.
  • El apilamiento paralelo en el registro de las fibrillas de alfa-sinucleína proporciona nuevos conocimientos sobre la patogénesis de la enfermedad de Parkinson.
  • Este método facilita los estudios estructurales de alta resolución de las fibrillas amiloides.