Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

NMR Spectroscopy: Spin–Spin Coupling01:08

NMR Spectroscopy: Spin–Spin Coupling

2.9K
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...
2.9K
¹H NMR: Long-Range Coupling01:27

¹H NMR: Long-Range Coupling

2.6K
The coupling interactions of nuclei across four or more bonds are usually weak, with J values less than 1 Hz. While these are usually not observed in spectra, the presence of multiple bonds along the coupling pathway can result in observable long-range coupling.
In alkenes, spin information is communicated via σ–π overlap, as seen in allylic (four-bond) and homoallylic (five-bond) couplings. These coupling interactions are stronger when the σ bond is parallel to the alkene...
2.6K
¹H NMR: Interpreting Distorted and Overlapping Signals01:02

¹H NMR: Interpreting Distorted and Overlapping Signals

1.4K
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...
1.4K
¹H NMR of Conformationally Flexible Molecules: Temporal Resolution00:52

¹H NMR of Conformationally Flexible Molecules: Temporal Resolution

1.2K
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...
1.2K
¹H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR01:15

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

1.6K
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.
1.6K
NMR Spectroscopy of Aromatic Compounds01:14

NMR Spectroscopy of Aromatic Compounds

6.1K
Aromatic compounds can be identified or analyzed using proton NMR and carbon‐13 NMR. Typically, aromatic hydrogens or hydrogens directly bonded to the aromatic rings are strongly deshielded by the aromatic ring current. Therefore, they absorb in the range of 6.5–8.0 ppm in proton NMR spectra. For instance, aromatic hydrogens directly bonded to the benzene ring absorb at 7.3 ppm. However, aromatic hydrogens of larger rings absorb farther upfield or downfield than the ideal range.
6.1K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Polystyrene Microplastics Activate Noncanonical TGF‑β Signaling and Metabolomic Reprogramming to Promote Epithelial-Mesenchymal Transition and Fibrosis in the Kidney.

ACS omega·2026
Same author

Using nature's blueprint porous organic polymeric nanotraps enables the interfacial activation of the hosted amine and CO<sub>2</sub>.

Nanoscale·2026
Same author

Dehydration-Induced Motional Heterogeneity in Native Collagen Protein Probed by Solid-State NMR Spectroscopy.

Biomacromolecules·2026
Same author

High-Resolution Proton NMR Spectra of NH Moieties in Solids Enabled by Offset-Tolerant Nitrogen-14 Decoupling via Fast Magic Angle Spinning at 70 kHz.

The journal of physical chemistry letters·2026
Same author

Attenuating Multispin Contributions during Selective Proton-Proton Distance Measurements in Magic Angle Spinning NMR.

The journal of physical chemistry letters·2025
Same author

A Longitudinal NMR-Based Metabolomics Highlights Shared Mechanisms of Pathophysiology in ARDS Patients With and Without Sepsis.

Magnetic resonance in chemistry : MRC·2025

Related Experiment Video

Updated: Jan 9, 2026

Preparation of Extracellular Matrix Protein Fibers for Brillouin Spectroscopy
07:19

Preparation of Extracellular Matrix Protein Fibers for Brillouin Spectroscopy

Published on: September 15, 2016

10.9K

Characterization of π-Interactions in Native Collagen by Solid-State NMR Spectroscopy.

Bijaylaxmi Patra1,2, Vipin Agarwal3, Neeraj Sinha1,2

  • 1Centre of Biomedical Research, SGPGIMS Campus, Raebareli Road, Lucknow 226014, India.

The Journal of Physical Chemistry. B
|December 9, 2025
PubMed
Summary
This summary is machine-generated.

Investigating bone collagen

More Related Videos

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

15.9K
Sample Preparation in Quartz Crystal Microbalance Measurements of Protein Adsorption and Polymer Mechanics
08:21

Sample Preparation in Quartz Crystal Microbalance Measurements of Protein Adsorption and Polymer Mechanics

Published on: January 22, 2020

14.1K

Related Experiment Videos

Last Updated: Jan 9, 2026

Preparation of Extracellular Matrix Protein Fibers for Brillouin Spectroscopy
07:19

Preparation of Extracellular Matrix Protein Fibers for Brillouin Spectroscopy

Published on: September 15, 2016

10.9K
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

15.9K
Sample Preparation in Quartz Crystal Microbalance Measurements of Protein Adsorption and Polymer Mechanics
08:21

Sample Preparation in Quartz Crystal Microbalance Measurements of Protein Adsorption and Polymer Mechanics

Published on: January 22, 2020

14.1K

Area of Science:

  • Biomaterials Science
  • Structural Biology
  • Biophysics

Background:

  • Collagen is crucial for bone strength and cohesion.
  • Its nanoscale organization in native bone ECM is poorly understood.
  • Collagen structure disruption is linked to diseases and aging.

Purpose of the Study:

  • To investigate collagen's nanoscale structure directly within the native bone matrix.
  • To uncover previously unresolved inter-residue correlations and potential stabilizing forces.
  • To provide insights into collagen structural stabilization in the native ECM.

Main Methods:

  • High-resolution fast magic-angle spinning (MAS) solid-state NMR (ssNMR) spectroscopy.
  • Two-dimensional (2D) 1H-detected 13C-1H double cross-polarization experiments at 70 kHz MAS.

Main Results:

  • Detected signals from low-abundance residues within the native bone matrix.
  • Uncovered previously unresolved inter-residue correlations in the aliphatic region.
  • Identified potential π-interactions between aromatic and other residues, suggesting additional stabilizing forces.

Conclusions:

  • Revealed previously missing insights into the chemico-physical basis of collagen structural stabilization.
  • Established a foundation for understanding disease-related structural changes in collagen.
  • Aids in designing biomimetic materials for tissue engineering applications.