Jove
Visualize
Contáctanos
JoVE
x logofacebook logolinkedin logoyoutube logo
ACERCA DE JoVE
Visión GeneralLiderazgoBlogCentro de Ayuda JoVE
AUTORES
Proceso de PublicaciónConsejo EditorialAlcance y PolíticasRevisión por ParesPreguntas FrecuentesEnviar
BIBLIOTECARIOS
TestimoniosSuscripcionesAccesoRecursosConsejo Asesor de BibliotecasPreguntas Frecuentes
INVESTIGACIÓN
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchivo
EDUCACIÓN
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualCentro de Recursos para ProfesoresSitio de Profesores
Términos y Condiciones de Uso
Política de Privacidad
Políticas

Videos de Conceptos Relacionados

NMR Spectrometers: Overview01:20

NMR Spectrometers: Overview

1.0K
NMR spectrometers consist of a strong magnet, a radiofrequency transmitter, and a detector attached to a computer console for recording spectra of samples containing NMR-active nuclei. In first-generation NMR instruments called continuous-wave spectrometers, the resonance frequencies of the nuclei are determined by frequency-sweep or field-sweep methods. The magnetic field strength is fixed and the rf signal is swept in the former, while the radiofrequency signal is fixed and the magnetic field...
1.0K
NMR Spectrometers: Resolution and Error Correction01:14

NMR Spectrometers: Resolution and Error Correction

658
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...
658
¹H NMR: Interpreting Distorted and Overlapping Signals01:02

¹H NMR: Interpreting Distorted and Overlapping Signals

1.0K
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...
1.0K
2D NMR: Overview of Homonuclear Correlation Techniques01:16

2D NMR: Overview of Homonuclear Correlation Techniques

166
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...
166
NMR Spectroscopy: Spin–Spin Coupling01:08

NMR Spectroscopy: Spin–Spin Coupling

1.2K
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...
1.2K
Chemical Shift: Internal References and Solvent Effects01:17

Chemical Shift: Internal References and Solvent Effects

599
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...
599

También podría leer

Artículos Relacionados

Artículos vinculados a este trabajo por autores compartidos, revista y gráfico de citas.

Ordenar por
Same author

In Vitro-Prepared A30P Alpha-Synuclein Fibrils Adopt the Conserved and Disease-Relevant Greek Key Fold.

The journal of physical chemistry. B·2026
Same author

Protonated Structure of EmrE Reveals C-terminal Tail Gating Mechanism.

bioRxiv : the preprint server for biology·2026
Same author

Probing Solution Dynamics of Tissue Factor Using Molecular Dynamics Simulations Guided by NMR Chemical Shifts.

The journal of physical chemistry. B·2026
Same author

<i>In vitro</i>-prepared A30P alpha-synuclein fibrils adopt the conserved and disease-relevant Greek key fold.

bioRxiv : the preprint server for biology·2026
Same author

Top-Down Scoring of Spectral Fitness by Image Analysis for Protein Structure Validation.

Journal of chemical information and modeling·2025
Same author

NMR Spectral Alignment Utilizing a CryoEM Motion Correction Algorithm.

Analytical chemistry·2025
Same journal

Decoding Galectin-Glycan Recognition with <sup>19</sup>F-Tagged Lectins: from Simple Glycans to the Cellular Glycocalyx.

Journal of the American Chemical Society·2026
Same journal

Open- and Closed-Shell Roles of Sensitizer and Annihilator in Pseudo-Single Component Mixtures for Upconversion.

Journal of the American Chemical Society·2026
Same journal

Pressure-Induced Superconductivity at 15 K in van-der-Waals Ferroelectric CuInP<sub>2</sub>S<sub>6</sub>.

Journal of the American Chemical Society·2026
Same journal

Carbene Analogues of Group 15: Reduction of s-Hydrindacene-Based Chloropnictogenium Ions To Access an Antimony Hydride Monocation and a Trinuclear Bismuth Dication.

Journal of the American Chemical Society·2026
Same journal

Chiral-Ligand-Modulated Nickel-Catalyzed Stereoselective Radical Migratory C2-Arylation of Carbohydrates.

Journal of the American Chemical Society·2026
Same journal

Coordination-Constraint-Driven Enhanced Chirality Induction in Perovskite Quantum Dot Solids.

Journal of the American Chemical Society·2026
Ver todos los artículos relacionados

Video Experimental Relacionado

Updated: Jun 2, 2025

NMR-Based Fragment Screening in a Minimum Sample but Maximum Automation Mode
09:19

NMR-Based Fragment Screening in a Minimum Sample but Maximum Automation Mode

Published on: June 4, 2021

3.2K

OPTO: Optimización automatizada para la espectroscopia de RMN en estado sólido

Collin G Borcik1,2, Barry DeZonia1,2, Thirupathi Ravula1,2

  • 1Department of Biochemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706, United States.

Journal of the American Chemical Society
|January 15, 2025
PubMed
Resumen
Este resumen es generado por máquina.

El software OPTO simplifica los experimentos de RMN de estado sólido (RMNM) mediante la automatización de la optimización de parámetros. Esto mejora la calidad y la accesibilidad de los datos para los investigadores que estudian sistemas biológicos y materiales complejos.

Más Videos Relacionados

15N CPMG Relaxation Dispersion for the Investigation of Protein Conformational Dynamics on the &#181;s-ms Timescale
08:09

15N CPMG Relaxation Dispersion for the Investigation of Protein Conformational Dynamics on the µs-ms Timescale

Published on: April 19, 2021

5.1K
NMR Spectroscopy as a Robust Tool for the Rapid Evaluation of the Lipid Profile of Fish Oil Supplements
08:54

NMR Spectroscopy as a Robust Tool for the Rapid Evaluation of the Lipid Profile of Fish Oil Supplements

Published on: May 1, 2017

26.0K

Videos de Experimentos Relacionados

Last Updated: Jun 2, 2025

NMR-Based Fragment Screening in a Minimum Sample but Maximum Automation Mode
09:19

NMR-Based Fragment Screening in a Minimum Sample but Maximum Automation Mode

Published on: June 4, 2021

3.2K
15N CPMG Relaxation Dispersion for the Investigation of Protein Conformational Dynamics on the &#181;s-ms Timescale
08:09

15N CPMG Relaxation Dispersion for the Investigation of Protein Conformational Dynamics on the µs-ms Timescale

Published on: April 19, 2021

5.1K
NMR Spectroscopy as a Robust Tool for the Rapid Evaluation of the Lipid Profile of Fish Oil Supplements
08:54

NMR Spectroscopy as a Robust Tool for the Rapid Evaluation of the Lipid Profile of Fish Oil Supplements

Published on: May 1, 2017

26.0K

Área de la Ciencia:

  • Espectroscopia de resonancia magnética nuclear de estado sólido (SSNMR)
  • Química biofísica
  • Ciencias de los materiales

Sus antecedentes:

  • SSNMR proporciona una visión única de los sistemas biológicos y materiales.
  • Las secuencias de pulso multidimensionales complejas son cruciales para las mediciones de resolución en el sitio en grandes biomoléculas.
  • La obtención de datos SSNMR reproducibles y de alta calidad es un desafío debido a la extensa capacitación del usuario y la difícil optimización de los parámetros.

Objetivo del estudio:

  • Para presentar OPTO, un entorno operativo de software diseñado para superar los desafíos de SSNMR.
  • Mejorar el rendimiento y la accesibilidad de los experimentos SSNMR de uso común.
  • Permitir una optimización fiable de las condiciones experimentales y mejorar la calidad de los datos.

Principales métodos:

  • Desarrollo de OPTO, un entorno de software con una interfaz gráfica de usuario.
  • Integración de algoritmos de optimización (simplex, búsqueda de cuadrícula) para el ajuste automatizado de parámetros.
  • Compatibilidad con las plataformas de software Varian OpenVnmrJ y Bruker Topspin.
  • Demostración de la optimización automatizada para el shimming, la polarización cruzada y otros parámetros experimentales.

Principales resultados:

  • Logró una anchura de línea de 12 partes por billón a través de la búsqueda global automatizada de 21 parámetros de parpadeo, mejorando la resolución.
  • Sensibilidad mejorada en experimentos de resonancia triple mediante la optimización de 16 parámetros para condiciones de polarización cruzada.
  • Robustez y reproducibilidad demostradas de los resultados a través de múltiples espectrómetros, intensidades de campo magnético y velocidades de giro de ángulo mágico utilizando muestras de proteínas.

Conclusiones:

  • El software OPTO aborda eficazmente los cuellos de botella en la adquisición y el análisis de datos del SSNMR.
  • El software aprovecha el tiempo del instrumento y permite a los operadores encontrar de manera confiable las condiciones experimentales óptimas.
  • OPTO facilita la generación de datos de SSNMR de alta calidad y reproducibles, avanzando en la investigación de la estructura, la dinámica y la función biomolecular.