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 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
Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

13.3K
Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
13.3K
Conservation of Protein Domains02:26

Conservation of Protein Domains

3.3K
3.3K
Protein Folding01:22

Protein Folding

123.5K
Overview
123.5K
Conserved Binding Sites01:49

Conserved Binding Sites

4.7K
Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
4.7K
Protein Organization01:24

Protein Organization

8.0K
Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence....
8.0K

You might also read

Related Articles

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

Sort by
Same author

Adhesion and polarity-driven morphogenesis: Mechanisms and constraints in tissue formation.

PLoS computational biology·2026
Same author

Modeling time to visual insight in Mooney image recognition with a chaotic recurrent neural network.

Cognitive neurodynamics·2026
Same author

Beyond variance: sensitivity-based dimensions in brain networks underlie individual differences in cognitive ability.

ArXiv·2026
Same author

The social dimension of apathy: evidence for a distinct domain from 11,243 individuals across health and neurocognitive disorders.

Translational psychiatry·2026
Same author

Unifying Constraints Linking Protein Folding and Native Dynamics Decoded from AlphaFold.

Physical review letters·2026
Same author

Enzyme as Maxwell's Demon: Steady-State Deviation from Chemical Equilibrium by Enhanced Enzyme Diffusion.

Physical review letters·2026
Same journal

Erratum: Bacterial Turbulence at Compressible Fluid Interfaces [Phys. Rev. Lett. 136, 138301 (2026)].

Physical review letters·2026
Same journal

Unveiling Light-Quark Yukawa Flavor Structure via Dihadron Fragmentation at Lepton Colliders.

Physical review letters·2026
Same journal

Adaptable Route to Fast Coherent State Transport via Bang-Bang-Bang Protocols.

Physical review letters·2026
Same journal

Topological Transition and Emergence of Elasticity of Dislocation in Skyrmion Lattice: Beyond Kittel's Magnetic-Polar Analogy.

Physical review letters·2026
Same journal

Pound-Drever-Hall Method for Superconducting-Qubit Readout.

Physical review letters·2026
Same journal

Coupling a ^{73}Ge Nuclear Spin to an Electrostatically Defined Quantum Dot in Silicon.

Physical review letters·2026
See all related articles

Related Experiment Video

Updated: Oct 20, 2025

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

15.6K

Dynamics-Evolution Correspondence in Protein Structures.

Qian-Yuan Tang1,2, Kunihiko Kaneko1

  • 1Center for Complex Systems Biology, Universal Biology Institute, University of Tokyo, Komaba 3-8-1, Meguro-ku, Tokyo 153-8902, Japan.

Physical Review Letters
|September 10, 2021
PubMed
Summary
This summary is machine-generated.

Protein dynamics correlate with structural variations, revealing a link between protein movement and evolution. This dynamics-evolution correspondence is crucial for understanding how proteins adapt and maintain flexibility over time.

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

2.3K
Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments
09:25

Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments

Published on: November 1, 2024

2.2K

Related Experiment Videos

Last Updated: Oct 20, 2025

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

15.6K
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
Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments
09:25

Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments

Published on: November 1, 2024

2.2K

Area of Science:

  • Structural biology
  • Protein dynamics
  • Evolutionary biology

Background:

  • Understanding the relationship between a protein's genetic makeup (genotype) and its physical characteristics (phenotype) is key in structural biology.
  • Investigating how protein structure and dynamics are influenced by genetic mutations and inherent molecular fluctuations is an ongoing challenge.

Purpose of the Study:

  • To quantitatively demonstrate the correlation between noise-induced protein dynamics and mutation-induced structural variations.
  • To elucidate the origin of the dynamics-evolution correspondence in proteins.
  • To explore the evolutionary mechanisms driving protein flexibility and structural variability.

Main Methods:

  • Analysis of a large dataset comprising proteins from hundreds of protein families.
  • Quantitative assessment of correlations between protein dynamics and structural variations.
  • Investigation of the linear responses of native proteins to understand underlying mechanisms.

Main Results:

  • A significant correlation was found between noise-induced protein dynamics and mutation-induced variations in native protein structures.
  • The study confirmed that both noise- and mutation-induced protein deformations are constrained within a common low-dimensional subspace.
  • Evidence supports a dynamics-evolution correspondence, linking protein flexibility to evolutionary adaptability.

Conclusions:

  • The findings elucidate the origin of the dynamics-evolution correspondence in proteins.
  • Proteins appear to evolve by maintaining a balance between dynamical flexibility and structural variability.
  • The identified low-dimensional subspace is critical for this evolutionary mechanism.