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

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

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

1.7K
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.
1.7K
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 Labile Protons: Temporal Resolution01:10

¹H NMR of Labile Protons: Temporal Resolution

1.7K
Protons bonded to heteroatoms such as nitrogen and oxygen exhibit a range of chemical shift values. This is due to the varying degree of hydrogen bonding between the proton and the heteroatom in other molecules. The extent of hydrogen bonding affects the electron density around the proton, thereby giving different chemical shift values for the protons in the proton NMR spectrum.
The –OH proton in alcohols typically appears in the range of δ 2 to 5 ppm but can vary depending on the specific...
1.7K

You might also read

Related Articles

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

Sort by
Same author

Toward a comprehensively characterized extract of Wharton's jelly extracellular matrix for the formulation of human collagen-based hydrogels.

International journal of pharmaceutics·2025
Same author

Characterization of Ultrasmall Superparamagnetic Iron Oxide via Fast Field-Cycling NMR Relaxometry at Two Temperatures.

Magnetic resonance in chemistry : MRC·2025
Same author

Supramolecular hydrogels derived from 2 : 1-[α/aza]-pseudopeptides: design, structural analysis and self-assembly in solution, solid, and gel states.

Journal of materials chemistry. B·2025
Same author

Heparinized collagen-based hydrogels for tissue engineering: physical, mechanical and biological properties.

International journal of pharmaceutics·2024
Same author

Nanoliposome functionalized colloidal GelMA inks for 3D printing of scaffolds with multiscale porosity.

Biofabrication·2024
Same author

Effect of the Dispersion Medium on NMR Relaxation Properties of Superparamagnetic Iron Oxide Nanoparticles between 0.24 mT and 14.1 T.

Langmuir : the ACS journal of surfaces and colloids·2024

Related Experiment Video

Updated: Jan 11, 2026

Transport Properties of Ibuprofen Encapsulated in Cyclodextrin Nanosponge Hydrogels: A Proton HR-MAS NMR Spectroscopy Study
10:10

Transport Properties of Ibuprofen Encapsulated in Cyclodextrin Nanosponge Hydrogels: A Proton HR-MAS NMR Spectroscopy Study

Published on: August 15, 2016

10.7K

Temperature Effect on Supramolecular Hydrogel Gelation Process: A High-Resolution and Fast-Field Cycling NMR Study.

Corentin Boulogne1, Gaëlle Cogneaux1, Paul Hoschtettler2

  • 1CRM2, Université de Lorraine, CNRS, Vandœuvre-lès-Nancy, France.

Magnetic Resonance in Chemistry : MRC
|November 14, 2025
PubMed
Summary
This summary is machine-generated.

Nuclear magnetic resonance (NMR) spectroscopy reveals how temperature affects peptide-based hydrogel formation and water dynamics. This study enhances understanding of hydrogel properties for biotechnological applications.

Keywords:
FFC 1H‐NMR relaxometrygelation kineticsnuclear magnetic resonance dispersion profilenucleopeptide hydrogel

More Related Videos

Combining Microfluidics and Microrheology to Determine Rheological Properties of Soft Matter during Repeated Phase Transitions
11:38

Combining Microfluidics and Microrheology to Determine Rheological Properties of Soft Matter during Repeated Phase Transitions

Published on: April 19, 2018

8.4K
Monitoring the Effects of Illumination on the Structure of Conjugated Polymer Gels Using Neutron Scattering
06:16

Monitoring the Effects of Illumination on the Structure of Conjugated Polymer Gels Using Neutron Scattering

Published on: December 21, 2017

6.0K

Related Experiment Videos

Last Updated: Jan 11, 2026

Transport Properties of Ibuprofen Encapsulated in Cyclodextrin Nanosponge Hydrogels: A Proton HR-MAS NMR Spectroscopy Study
10:10

Transport Properties of Ibuprofen Encapsulated in Cyclodextrin Nanosponge Hydrogels: A Proton HR-MAS NMR Spectroscopy Study

Published on: August 15, 2016

10.7K
Combining Microfluidics and Microrheology to Determine Rheological Properties of Soft Matter during Repeated Phase Transitions
11:38

Combining Microfluidics and Microrheology to Determine Rheological Properties of Soft Matter during Repeated Phase Transitions

Published on: April 19, 2018

8.4K
Monitoring the Effects of Illumination on the Structure of Conjugated Polymer Gels Using Neutron Scattering
06:16

Monitoring the Effects of Illumination on the Structure of Conjugated Polymer Gels Using Neutron Scattering

Published on: December 21, 2017

6.0K

Area of Science:

  • Biomaterials Science
  • Soft Matter Physics
  • Biotechnology

Background:

  • Peptide-based supramolecular hydrogels offer biocompatibility and tunable properties for diverse biotechnological uses.
  • Grafting nucleobases and employing multicomponent strategies allow fine-tuning of hydrogel characteristics.
  • Understanding hydrogel behavior at the atomic level is crucial for optimizing their applications.

Purpose of the Study:

  • To investigate the gelation process of peptide-based hydrogels using nuclear magnetic resonance (NMR) spectroscopy.
  • To explore the influence of temperature on hydrogel formation and internal water dynamics.
  • To gain atomic-level insights into the transition from solution to gel states.

Main Methods:

  • High-resolution NMR and fast-field cycling NMR relaxation were employed to study gelator signals and water dynamics during gelation.
  • NMR dispersion profiles were analyzed to identify and characterize different water pools and their mobility within the hydrogel matrix.
  • Experiments were conducted at two distinct temperatures (295 K and 313 K) to assess thermal effects.

Main Results:

  • NMR relaxation measurements provided insights into the gelator's behavior and water dynamics throughout the gelation process.
  • Analysis of NMR dispersion profiles revealed distinct water populations and their varying mobilities within the hydrogel.
  • Temperature variations significantly impacted the gelation kinetics and the dynamical behavior of water molecules within the hydrogel structure.

Conclusions:

  • NMR spectroscopy is a powerful tool for elucidating the mechanisms of hydrogel formation and the role of water dynamics.
  • Temperature plays a critical role in modulating both the gelation process and the solvent's behavior within the supramolecular network.
  • This research provides fundamental understanding for designing advanced peptide-based hydrogels with tailored properties for specific applications.