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Related Concept Videos

¹H NMR: Interpreting Distorted and Overlapping Signals01:02

¹H NMR: Interpreting Distorted and Overlapping Signals

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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...
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NMR Spectrometers: Resolution and Error Correction01:14

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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...
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Atomic Nuclei: Nuclear Relaxation Processes01:23

Atomic Nuclei: Nuclear Relaxation Processes

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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.
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Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

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Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
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¹H NMR: Complex Splitting01:13

¹H NMR: Complex Splitting

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A proton M that is coupled to a proton X results in doublet signals for M. However, NMR-active nuclei can be simultaneously coupled to more than one nonequivalent nucleus. When M is coupled to a second proton A, such as in styrene oxide, each peak in the doublet is split into another doublet.
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¹H NMR of Conformationally Flexible Molecules: Temporal Resolution00:52

¹H NMR of Conformationally Flexible Molecules: Temporal Resolution

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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...
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Updated: Nov 6, 2025

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins
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Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins

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NMR illuminates intrinsic disorder.

H Jane Dyson1, Peter E Wright1

  • 1Department of Integrative Structural and Computational Biology and Skaggs Institute of Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, 92037, California, USA.

Current Opinion in Structural Biology
|May 5, 2021
PubMed
Summary
This summary is machine-generated.

Nuclear magnetic resonance (NMR) is crucial for studying intrinsically disordered proteins (IDPs) and their regions (IDRs). This technique, combined with others, reveals insights into protein structure, dynamics, and disease-related aggregation.

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Area of Science:

  • Biophysics
  • Structural Biology
  • Biochemistry

Background:

  • Intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs) lack stable tertiary structures.
  • These regions are implicated in various diseases, including Alzheimer's, Parkinson's, and Huntington's diseases.
  • Understanding IDP behavior is critical for deciphering disease mechanisms.

Purpose of the Study:

  • To highlight the continued importance and evolving applications of Nuclear Magnetic Resonance (NMR) in characterizing IDPs and IDRs.
  • To showcase how NMR, in conjunction with other biophysical techniques, provides comprehensive insights into IDP structure and function.
  • To emphasize NMR's role in understanding disease-related protein misfolding and aggregation.

Main Methods:

  • Nuclear Magnetic Resonance (NMR) spectroscopy.
  • Integration of NMR with complementary biophysical methods like small-angle scattering, single-molecule fluorescence, EPR, and mass spectrometry.
  • Advanced NMR techniques for analyzing complex protein sequences and interactions.

Main Results:

  • NMR provides detailed insights into the solution structure, dynamics, and functional mechanisms of IDPs and IDRs.
  • Recent advances enable characterization of proteins with mixed ordered/disordered domains and repetitive sequences.
  • Innovative NMR applications illuminate protein aggregation pathways and target interactions.

Conclusions:

  • NMR remains an invaluable tool for studying the complex nature of IDPs and IDRs.
  • The combination of NMR with other methods offers a powerful approach to understanding protein behavior in solution.
  • NMR-driven insights are crucial for advancing our knowledge of protein misfolding diseases.