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

Applications Of NMR In Biology01:25

Applications Of NMR In Biology

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.
The...
Fast Reactions01:27

Fast Reactions

Fast reactions occurring in times shorter than the time needed to mix reactants pose a unique challenge for investigation. In a liquid-phase continuous-flow system, reactants A and B are swiftly pushed into the mixing chamber, where mixing occurs within 1 ms. The reaction mixture then flows through an observation tube, and one measures light absorption to determine species concentrations at various points of the tube. This method is most appropriate when relatively large volumes of reactants...
Protein Dynamics in Living Cells01:19

Protein Dynamics in Living Cells

Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...
¹H NMR of Conformationally Flexible Molecules: Temporal Resolution00:52

¹H NMR of Conformationally Flexible Molecules: Temporal Resolution

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...
NMR Spectrometers: Radiofrequency Pulses and Pulse Sequences01:17

NMR Spectrometers: Radiofrequency Pulses and Pulse Sequences

A pulse is a short burst of radio waves distributed over a range of frequencies that simultaneously excites all the nuclei in the sample. Upon passing a radio frequency pulse along the x-axis, the nuclei absorb energy corresponding to their Larmor frequencies and achieve resonance. This shifts the net magnetization vector from the z-axis toward the transverse plane. This angle of rotation of the magnetization vector, or the flip angle, is proportional to the duration and intensity of the pulse.
Double Resonance Techniques: Overview01:12

Double Resonance Techniques: Overview

Double resonance techniques in Nuclear Magnetic Resonance (NMR) spectroscopy involve the simultaneous application of two different frequencies or radiofrequency pulses to manipulate and observe two distinct nuclear spins. One important application of double resonance is spin decoupling, which selectively suppresses coupling with one type of nucleus while observing the NMR signal from another nucleus, simplifying the spectrum and enhancing resolution.
Spin decoupling is usually achieved by...

You might also read

Related Articles

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

Sort by
Same author

Disordered N-Terminal Tail "Wags the Dog" in Human Thymidylate Synthase.

Biochemistry·2026
Same author

The Power of Protein Dynamics in Binding and Allostery.

Biochemistry·2026
Same author

A flexible, allosteric loop regulates protein activity and rewires electrostatics.

Protein science : a publication of the Protein Society·2025
Same author

Mixed, nonclassical behavior in a classic allosteric protein.

Proceedings of the National Academy of Sciences of the United States of America·2023
Same author

Allosteric inactivation of an engineered optogenetic GTPase.

Proceedings of the National Academy of Sciences of the United States of America·2023
Same author

Dynamic allostery in substrate binding by human thymidylate synthase.

eLife·2022

Related Experiment Video

Updated: Jun 8, 2026

NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins
09:25

NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins

Published on: November 1, 2024

Using NMR to study fast dynamics in proteins: methods and applications.

Paul J Sapienza1, Andrew L Lee

  • 1Division of Medicinal Chemistry & Natural Products, Eshelman School of Pharmacy, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.

Current Opinion in Pharmacology
|October 12, 2010
PubMed
Summary
This summary is machine-generated.

Protein dynamics are crucial for function and drug design. Nuclear Magnetic Resonance (NMR) spectroscopy reveals these picosecond-nanosecond timescale motions using order parameters, linking dynamics to protein function.

More Related Videos

Study of Protein Dynamics via Neutron Spin Echo Spectroscopy
08:03

Study of Protein Dynamics via Neutron Spin Echo Spectroscopy

Published on: April 13, 2022

15N CPMG Relaxation Dispersion for the Investigation of Protein Conformational Dynamics on the µs-ms Timescale
08:09

15N CPMG Relaxation Dispersion for the Investigation of Protein Conformational Dynamics on the µs-ms Timescale

Published on: April 19, 2021

Related Experiment Videos

Last Updated: Jun 8, 2026

NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins
09:25

NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins

Published on: November 1, 2024

Study of Protein Dynamics via Neutron Spin Echo Spectroscopy
08:03

Study of Protein Dynamics via Neutron Spin Echo Spectroscopy

Published on: April 13, 2022

15N CPMG Relaxation Dispersion for the Investigation of Protein Conformational Dynamics on the µs-ms Timescale
08:09

15N CPMG Relaxation Dispersion for the Investigation of Protein Conformational Dynamics on the µs-ms Timescale

Published on: April 19, 2021

Area of Science:

  • Biochemistry
  • Structural Biology
  • Biophysics

Background:

  • Proteins are dynamic entities, not static structures, existing in numerous conformational substates.
  • Understanding these protein dynamics is essential for comprehending protein function and for structure-based drug design.
  • Nuclear Magnetic Resonance (NMR) spectroscopy is a powerful technique for studying molecular dynamics in solution at atomic resolution.

Purpose of the Study:

  • To review Nuclear Magnetic Resonance (NMR) relaxation methods for characterizing protein thermal motions on the picosecond-nanosecond (ps-ns) timescale.
  • To discuss the Lipari-Szabo order parameter (S²) as a measure of restricted motion on the ps-ns timescale.
  • To highlight the connection between ps-ns protein dynamics and key biological concepts like conformational entropy and allostery.

Main Methods:

  • Utilizing NMR relaxation techniques to probe molecular motions.
  • Applying the Lipari-Szabo order parameter (S²) to quantify restricted bond motion.
  • Analyzing literature examples that correlate ps-ns dynamics with functional properties.

Main Results:

  • NMR relaxation methods effectively characterize ps-ns timescale protein dynamics.
  • The Lipari-Szabo order parameter (S²) provides a quantitative measure of motion restriction.
  • Ps-ns dynamics are demonstrably linked to conformational entropy, allostery, and overall protein function.

Conclusions:

  • NMR spectroscopy is a key tool for elucidating protein dynamics.
  • Understanding ps-ns dynamics is critical for advancing our knowledge of protein function and drug discovery.
  • The Lipari-Szabo order parameter is a valuable metric for characterizing these dynamics.