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: 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

1.7K
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

You might also read

Related Articles

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

Sort by
Same author

Real-world evaluation of access-driven Canadian treatment sequences in progressive prostate cancer (REACTIVATE).

Canadian Urological Association journal = Journal de l'Association des urologues du Canada·2024
Same author

Real-world evaluation of access-driven Canadian treatment sequences in progressive prostate cancer (REACTIVATE).

Canadian Urological Association journal = Journal de l'Association des urologues du Canada·2024
Same author

Efficacy, tolerability, and endometrial safety of ospemifene compared with current therapies for the treatment of vulvovaginal atrophy: a systematic literature review and network meta-analysis.

Menopause (New York, N.Y.)·2023
Same author

Biological Networks across Scales-The Theoretical and Empirical Foundations for Time-Varying Complex Networks that Connect Structure and Function across Levels of Biological Organization.

Integrative and comparative biology·2021
Same author

Short-term efficacy of latanoprostene bunod for the treatment of open-angle glaucoma and ocular hypertension: a systematic literature review and a network meta-analysis.

The British journal of ophthalmology·2021
Same author

Congressional Budget Responses to the Pandemic: Fund Health Care, Not Warfare.

American journal of public health·2020

Related Experiment Video

Updated: Jan 11, 2026

High-Pressure NMR Experiments for Detecting Protein Low-Lying Conformational States
04:37

High-Pressure NMR Experiments for Detecting Protein Low-Lying Conformational States

Published on: June 29, 2021

3.1K

Mapping Protein Conformational Landscapes with High-Pressure NMR.

Catherine Royer1

  • 1Department of Biological Sciences, Rensselaer Polytechnic Institute, Troy, New York, USA;

Annual Review of Biophysics
|November 18, 2025
PubMed
Summary
This summary is machine-generated.

High-pressure nuclear magnetic resonance (HP NMR) maps protein stability and dynamics by analyzing pressure-induced unfolding and conformational landscapes. This technique reveals how protein sequences influence excited states crucial for function.

Keywords:
NMRconformational landscapeshigh pressuresequence determinantsvolume changes

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
Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web
09:51

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

Published on: July 16, 2017

16.0K

Related Experiment Videos

Last Updated: Jan 11, 2026

High-Pressure NMR Experiments for Detecting Protein Low-Lying Conformational States
04:37

High-Pressure NMR Experiments for Detecting Protein Low-Lying Conformational States

Published on: June 29, 2021

3.1K
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
Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web
09:51

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

Published on: July 16, 2017

16.0K

Area of Science:

  • Biophysics
  • Structural Biology
  • Protein Science

Background:

  • Understanding protein stability and conformational dynamics is key to deciphering protein function.
  • High pressure is a powerful tool to perturb protein structures and study their response.
  • Nuclear Magnetic Resonance (NMR) spectroscopy offers atomic-level insights into protein structure and dynamics.

Purpose of the Study:

  • To review the application of high-pressure nuclear magnetic resonance (HP NMR) in protein science.
  • To highlight HP NMR's capability in mapping local protein stability and conformational landscapes.
  • To emphasize the study of protein excited states and their sequence determinants.

Main Methods:

  • Utilizing high-pressure nuclear magnetic resonance (HP NMR) to probe protein behavior.
  • Analyzing pressure-temperature phase diagrams to understand volumetric properties and unfolding.
  • Investigating pressure-induced equilibrium unfolding and conformational heterogeneity.

Main Results:

  • HP NMR effectively maps local protein stability and conformational landscapes.
  • The technique reveals the population and characteristics of protein excited states.
  • Sequence determinants influencing these landscapes and functional dynamics are identified.

Conclusions:

  • HP NMR is a valuable method for characterizing protein conformational heterogeneity and stability.
  • Understanding excited states through HP NMR is critical for resolving fundamental questions in protein science.
  • This approach provides insights into the sequence-based control of protein functional dynamics.