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

Protein Diffusion in the Membrane01:24

Protein Diffusion in the Membrane

5.0K
Proteins show rotational as well as lateral diffusion across the membrane. The lateral diffusion of proteins was confirmed through the cell fusion experiment where mouse and human cells were fused, resulting in hybrid cells. When the human and mouse cells fused, the specific membrane proteins on human and mouse cells were marked with the red and green-fluorescent markers, respectively. Initially, the red and green fluorescence was located on the respective hemisphere of the cell. As time...
5.0K
Protein Dynamics in Living Cells01:19

Protein Dynamics in Living Cells

2.4K
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...
2.4K

You might also read

Related Articles

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

Sort by
Same author

Human Substance P Interactions with G Protein-Coupled Receptor NK1R Observed by NMR in Solution.

Journal of the American Chemical Society·2025
Same author

Meet the authors: Canyong Guo and Kurt Wüthrich.

Cell chemical biology·2025
Same author

Structural basis of adenosine 2A receptor-balanced signaling activation relies on allosterically mediated structural dynamics.

Cell chemical biology·2025
Same author

Rimota-Gd: Paramagnetic Probe for In Vivo MRI Studies of the Cannabinoid 1 Receptor Distribution in the Mouse Brain.

ACS chemical neuroscience·2024
Same author

Reflections from Nobel laureates in chemistry.

Cell chemical biology·2024
Same author

Fluorine-19 labeling of the tryptophan residues in the G protein-coupled receptor NK1R using the 5-fluoroindole precursor in Pichia pastoris expression.

Journal of biomolecular NMR·2024
Same journal

Localization-driven exchange contrast in diffusion exchange spectroscopy.

Journal of magnetic resonance (San Diego, Calif. : 1997)·2026
Same journal

4.5 Tesla superconducting miniature magnet in liquid nitrogen.

Journal of magnetic resonance (San Diego, Calif. : 1997)·2026
Same journal

Folding and unfolding dynamics of a DNA aptamer studied by heteronuclear <sup>1</sup>H-<sup>13</sup>C correlation zz-exchange spectroscopy.

Journal of magnetic resonance (San Diego, Calif. : 1997)·2026
Same journal

Multi-spin control from one-spin pulses.

Journal of magnetic resonance (San Diego, Calif. : 1997)·2026
Same journal

Altering MRI rotating frame relaxations by changing the truncation level of Hyperbolic Secant pulse.

Journal of magnetic resonance (San Diego, Calif. : 1997)·2026
Same journal

Effects of proton exchange on the lifetimes of long-lived states in aliphatic chains.

Journal of magnetic resonance (San Diego, Calif. : 1997)·2026
See all related articles

Related Experiment Video

Updated: Oct 24, 2025

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

2.3K

Brownian motion, spin diffusion and protein structure determination in solution.

Kurt Wüthrich1

  • 1ETH Zürich, Zürich Switzerland and Scripps Research, La Jolla, CA, USA.

Journal of Magnetic Resonance (San Diego, Calif. : 1997)
|August 15, 2021
PubMed
Summary
This summary is machine-generated.

This work details the development of Nuclear Magnetic Resonance (NMR) for protein structure determination in solution. Key advancements enabled precise spatial arrangement mapping of polypeptide chains using interatomic distance measurements.

Keywords:
Distance geometryHigh-field NMRMulti-dimensional NMRNuclear Overhauser effect (NOE)Protein dynamicsProteins in solutionSequence-specific resonance assignmentSequential resonance assignmentStructural biology

More Related Videos

In Situ Monitoring of Diffusion of Guest Molecules in Porous Media Using Electron Paramagnetic Resonance Imaging
06:34

In Situ Monitoring of Diffusion of Guest Molecules in Porous Media Using Electron Paramagnetic Resonance Imaging

Published on: September 2, 2016

6.5K
High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water
08:48

High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water

Published on: April 28, 2022

1.9K

Related Experiment Videos

Last Updated: Oct 24, 2025

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

2.3K
In Situ Monitoring of Diffusion of Guest Molecules in Porous Media Using Electron Paramagnetic Resonance Imaging
06:34

In Situ Monitoring of Diffusion of Guest Molecules in Porous Media Using Electron Paramagnetic Resonance Imaging

Published on: September 2, 2016

6.5K
High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water
08:48

High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water

Published on: April 28, 2022

1.9K

Area of Science:

  • Biochemistry
  • Structural Biology
  • Biophysics

Background:

  • Protein structure determination is crucial for understanding biological function.
  • Nuclear Magnetic Resonance (NMR) in solution offers a unique approach to study protein dynamics.
  • Early methods faced limitations in resolving complex molecular structures.

Purpose of the Study:

  • To recount the historical development of NMR-based protein structure determination from 1968 to 1992.
  • To highlight key methodological innovations enabling atomic-resolution structural analysis.
  • To establish NMR as a viable technique for protein structure elucidation in solution.

Main Methods:

  • Utilizing Nuclear Overhauser Effect (NOE) for interatomic distance measurements between hydrogen atoms.
  • Developing sequence-specific resonance assignment to overcome the 'phase problem'.
  • Implementing novel distance geometry algorithms for structure calculation from NMR constraints.
  • Employing two-dimensional NMR for enhanced spectral resolution and connectivity analysis.

Main Results:

  • Demonstrated that short proton-proton distances, measured via NOE, provide atomic-resolution structures.
  • Established sequence-specific resonance assignment as a critical step for NMR structure determination.
  • Validated distance geometry calculations for predicting protein structures from experimental data.
  • Showcased 2D NMR's capability to resolve complex protein spectra and map connectivities.

Conclusions:

  • The integration of NOE, resonance assignment, distance geometry, and 2D NMR made protein structure determination in solution feasible and attractive.
  • These advancements significantly contributed to the field of structural biology, enabling detailed insights into protein architecture.
  • The described period (1968-1992) represents a foundational era for modern solution NMR structural biology.