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Related Concept Videos

Globular and Fibrous Proteins02:21

Globular and Fibrous Proteins

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Many proteins can be classified into two distinct subtypes - globular or fibrous. These two types differ in their shapes and solubilities.
Globular proteins are also known as spheroproteins and typically are approximately round in shape. They contain a mix of amino acid types and contain differing sequences in their primary structures. Globular proteins have many different functions, such as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be...
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Nuclear Magnetic Resonance (NMR): Overview01:07

Nuclear Magnetic Resonance (NMR): Overview

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Nuclear magnetic resonance (NMR) is a phenomenon exhibited by certain nuclei that can absorb characteristic radio frequency radiation under certain conditions. NMR has been extensively applied in molecular spectroscopy and medical diagnostic imaging. In both these applications, the molecule or subject under study is placed in a magnetic field and irradiated with radio frequency energy.
NMR spectroscopy generates a spectrum where the characteristic absorption frequencies of the sample are...
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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.
Splitting diagrams or splitting tree diagrams are routinely used to depict such complex couplings. While drawing splitting diagrams, the splitting with the larger coupling constant is usually applied...
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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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NMR Spectroscopy: Spin–Spin Coupling01:08

NMR Spectroscopy: Spin–Spin Coupling

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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...
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¹H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR01:15

¹H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR

1.4K
The axial and equatorial protons in cyclohexane can be distinguished by performing a variable-temperature NMR experiment. In this process, except for one proton, the remaining eleven protons are replaced by deuterium. The deuterium substitution avoids the possible peak splitting caused by the spin-spin coupling between the adjacent protons. The remaining proton flips between the axial and equatorial positions.
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Related Experiment Video

Updated: May 3, 2026

15N CPMG Relaxation Dispersion for the Investigation of Protein Conformational Dynamics on the &#181;s-ms Timescale
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Modeling Protein Aggregation Kinetics from NMR Data.

Vitali Tugarinov1, Francesco Torricella1, Shreya Ghosh1

  • 1Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0520, USA.

Journal of Molecular Biology
|June 11, 2025
PubMed
Summary
This summary is machine-generated.

This study details using Nuclear Magnetic Resonance (NMR) spectroscopy to track protein aggregation kinetics. It models aggregation processes, offering insights into diseases like Huntington's and Alzheimer's.

Keywords:
Huntington’s diseaseNMR fast acquisition methodsNMR spin relaxationprotein aggregation kineticsβ-amyloid fibril formation

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Area of Science:

  • Biochemistry
  • Biophysics
  • Structural Biology

Background:

  • Protein aggregation is implicated in neurodegenerative diseases.
  • Understanding aggregation kinetics is crucial for therapeutic development.

Purpose of the Study:

  • To present practical methods for using NMR spectroscopy to monitor protein aggregation.
  • To quantitatively model the kinetics of protein aggregation and inhibition.

Main Methods:

  • Utilizing fast two-dimensional 1H-15N correlation NMR spectra.
  • Applying kinetic modeling to NMR data for aggregation processes.
  • Studying huntingtin exon-1 and amyloid-beta 42 aggregation.

Main Results:

  • Demonstrated quantitative modeling of protein aggregation kinetics via NMR.
  • Provided examples of aggregation kinetics for huntingtin exon-1 and amyloid-beta 42.
  • Illustrated the mechanism of inhibition by the chaperone Hsp104.

Conclusions:

  • NMR spectroscopy is a powerful tool for studying protein aggregation kinetics.
  • Kinetic modeling of NMR data enables quantitative analysis of aggregation processes.
  • This approach aids in understanding disease mechanisms and developing inhibitors.