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Videos de Conceptos Relacionados

¹H NMR of Conformationally Flexible Molecules: Temporal Resolution00:52

¹H NMR of Conformationally Flexible Molecules: Temporal Resolution

At room temperature, the chair conformer of cyclohexane undergoes rapid ring flipping between two equivalent chair conformers at a rate of approximately 105 times per second. These two chair conformers are in equilibrium. The rapid ring flipping results in the interconversion of the axial proton to an equatorial proton and an equatorial to the axial proton. Such interconversions are too rapid and cannot be detected on the NMR timescale. Hence, the NMR spectrometer cannot distinguish between the...
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...
Atomic Nuclei: Nuclear Relaxation Processes01:23

Atomic Nuclei: Nuclear Relaxation Processes

In the absence of an external magnetic field, nuclear spin states are degenerate and randomly oriented. When a magnetic field is applied, the spins begin to precess and orient themselves along (lower energy) or against (higher energy) the direction of the field. At equilibrium, a slight excess population of spins exists in the lower energy state. Because the direction of the magnetic field is fixed as the z-axis,  the precessing magnetic moments are randomly oriented around the z-axis. This...
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...
Atomic Nuclei: Types of Nuclear Relaxation01:28

Atomic Nuclei: Types of Nuclear Relaxation

Nuclear relaxation restores the equilibrium population imbalance and can occur via spin–lattice or spin–spin mechanisms, which are first-order exponential decay processes.
In spin–lattice or longitudinal relaxation, the excited spins exchange energy with the surrounding lattice as they return to the lower energy level. Among several mechanisms that contribute to spin–lattice relaxation, magnetic dipolar interactions are significant. Here, the excited nucleus transfers energy to a nearby...
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...

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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

Mapeo del auto-reconocimiento del polipéptido a través de la relajación de (1) H fuera de resonancia.

Veronica Esposito1, Rahul Das, Giuseppe Melacini

  • 1Departments of Chemistry, Biochemistry and Biomedical Sciences, McMaster University, 1280 Main Street W., Hamilton, Ontario L8S 4M1, Canada.

Journal of the American Chemical Society
|June 30, 2005
PubMed
Resumen

Este estudio introduce un nuevo método de resonancia magnética nuclear (RMN) para mapear con precisión las interacciones débiles en la fibrilogénesis amiloide. La técnica supera los desafíos experimentales, ayudando al estudio de los péptidos amiloidogénicos y las interacciones proteína-ligando.

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Área de la Ciencia:

  • Química biofísica y bioquímica.
  • Biología Estructural Biología estructural.
  • La neurociencia es la neurociencia.

Sus antecedentes:

  • Las tasas de relajación de la resonancia magnética nuclear (RMN) son sensibles a las interacciones moleculares débiles, cruciales para comprender la oligomerización de polipéptidos en la fibrilogénesis amiloide.
  • Los métodos tradicionales de RMN para medir las tasas de relajación se enfrentan a desafíos experimentales, incluidos los problemas de transferencia J y selectividad, lo que dificulta el estudio de la formación de amiloide en etapa temprana.
  • La fibrilogénesis amiloide, implicada en enfermedades neurodegenerativas, implica interacciones polipéptidas complejas que son difíciles de caracterizar.

Objetivo del estudio:

  • Desarrollar y validar un nuevo enfoque basado en RMN para superar las limitaciones experimentales en la medición de las tasas de relajación para las interacciones débiles.
  • Aplicar este método para mapear las interacciones de auto-reconocimiento en el péptido amiloide-beta (Abeta) (12-28).
  • Demostrar la amplia aplicabilidad de la técnica para estudiar los péptidos amiloidogénicos y las interacciones proteína-ligando.

Principales métodos:

  • Medición de las tasas de relajación no selectiva fuera de resonancia 1H utilizando un campo efectivo inclinado en 35,5 grados.
  • Eludir la transferencia J y los problemas de selectividad inherentes a los experimentos Carr-Purcell-Meiboom-Gill (CPMG) y de recuperación por inversión.
  • Aplicación a los spins Halpha del péptido Abeta (12-28) para generar un mapa de resolución de residuos.

Principales resultados:

  • El experimento de RMN propuesto efectivamente elude los desafíos experimentales asociados con las mediciones tradicionales de la tasa de relajación.
  • Se generó un mapa de auto-reconocimiento de resolución de residuos para el péptido Abeta (12-28).
  • El mapa obtenido es consistente con los hallazgos de estudios mutacionales independientes, validando la precisión del método.

Conclusiones:

  • La nueva técnica de RMN proporciona un método robusto y sensible para investigar las interacciones débiles en la oligomerización de polipéptidos.
  • Este enfoque es muy valioso para estudiar las primeras etapas de la fibrilogénesis amiloide y caracterizar los péptidos amiloidogénicos.
  • El método es ampliamente aplicable para el cribado y el mapeo de las interacciones proteína-ligando, ofreciendo un potencial significativo en el descubrimiento de fármacos y la biología estructural.