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¹H NMR: Interpreting Distorted and Overlapping Signals01:02

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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.
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Noncovalent Attractions in Biomolecules02:35

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Noncovalent attractions are associations within and between molecules that influence the shape and structural stability of complexes. These interactions differ from covalent bonding in that they do not involve sharing of electrons.
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NMR Spectroscopy: Spin–Spin Coupling01:08

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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: Temporal Resolution00:52

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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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Applications Of NMR In Biology01:25

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Nuclear magnetic resonance (NMR) spectroscopy is a very valuable analytical technique for researchers. It has been used for more than 50 years as an analytical tool. F. Bloch and E. Purcell formulated NMR in 1946 and won the 1952 Nobel Prize in Physics  for their work. Biological macromolecules such as proteins, nucleic acids, lipids, and organic molecules including pharmaceutical compounds, can be studied using this versatile tool that exploits the magnetic properties of certain nuclei.
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Related Experiment Video

Updated: Mar 17, 2026

Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments
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Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments

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Intermolecular Interactions and Protein Dynamics by Solid-State NMR Spectroscopy.

Jonathan M Lamley1, Carl Öster1, Rebecca A Stevens1

  • 1Department of Chemistry, University of Warwick, Gibbet Hill Road, Coventry CV4 7AL (UK).

Angewandte Chemie (Weinheim an Der Bergstrasse, Germany)
|August 2, 2016
PubMed
Summary
This summary is machine-generated.

Protein dynamics in crystalline GB1 and GB1-antibody complexes were studied. Slow motions were more prevalent in the complex, suggesting potential anisotropic motion at the interaction interface.

Keywords:
NMR‐SpektroskopieProteindynamikProtein‐Antikörper‐KomplexeProtein‐Protein‐WechselwirkungenRotation um den magischen Winkel

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Area of Science:

  • Biophysics
  • Protein dynamics
  • Structural biology

Background:

  • Understanding protein dynamics is essential for biophysical processes.
  • Protein GB1 dynamics were investigated in crystalline and antibody-complex forms.

Purpose of the Study:

  • To investigate backbone dynamics of protein GB1 in different assemblies.
  • To compare dynamics across a wide timescale (picoseconds to microseconds).

Main Methods:

  • Site-specific 15N relaxation rates and relaxation dispersion measurements.
  • Analysis of protein dynamics in crystalline GB1 and GB1-antibody complexes.
  • Utilized samples with as little as eight nanomoles of GB1.

Main Results:

  • Fast picosecond-nanosecond motions were conserved between crystalline GB1 and the complex.
  • Slow motions (>500 ns) were significantly more prevalent in the GB1-antibody complex.
  • Data suggest GB1 may exhibit anisotropic motion at the interaction interface within the complex.

Conclusions:

  • Protein dynamics are influenced by assembly state, particularly slow motions.
  • GB1's dynamic behavior differs between crystalline and complexed states.
  • Potential for anisotropic motion in GB1 within antibody complexes identified.