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Related Concept Videos

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

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Published on: September 17, 2017

Mapping polypeptide self-recognition through (1)H off-resonance relaxation.

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
Summary

This study introduces a novel nuclear magnetic resonance (NMR) method to precisely map weak interactions in amyloid fibrillogenesis. The technique overcomes experimental challenges, aiding the study of amyloidogenic peptides and protein-ligand interactions.

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Area of Science:

  • Biophysical Chemistry
  • Structural Biology
  • Neuroscience

Background:

  • Nuclear magnetic resonance (NMR) relaxation rates are sensitive to weak molecular interactions, crucial for understanding polypeptide oligomerization in amyloid fibrillogenesis.
  • Traditional NMR methods for measuring relaxation rates face experimental challenges, including J-transfer and selectivity issues, hindering the study of early-stage amyloid formation.
  • Amyloid fibrillogenesis, implicated in neurodegenerative diseases, involves complex polypeptide interactions that are difficult to characterize.

Purpose of the Study:

  • To develop and validate a novel NMR-based approach to overcome experimental limitations in measuring relaxation rates for weak interactions.
  • To apply this method to map self-recognition interactions in the amyloid-beta (Abeta) (12-28) peptide.
  • To demonstrate the broad applicability of the technique for studying amyloidogenic peptides and protein-ligand interactions.

Main Methods:

  • Measurement of nonselective off-resonance 1H relaxation rates using an effective field tilted by 35.5 degrees.
  • Circumvention of J-transfer and selectivity problems inherent in Carr-Purcell-Meiboom-Gill (CPMG) and inversion-recovery experiments.
  • Application to the Halpha spins of the Abeta (12-28) peptide to generate a residue-resolution map.

Main Results:

  • The proposed NMR experiment effectively circumvents experimental challenges associated with traditional relaxation rate measurements.
  • A residue-resolution self-recognition map for the Abeta (12-28) peptide was generated.
  • The obtained map is consistent with findings from independent mutational studies, validating the method's accuracy.

Conclusions:

  • The novel NMR technique provides a robust and sensitive method for investigating weak interactions in polypeptide oligomerization.
  • This approach is highly valuable for studying the early stages of amyloid fibrillogenesis and characterizing amyloidogenic peptides.
  • The method is broadly applicable for screening and mapping protein-ligand interactions, offering significant potential in drug discovery and structural biology.