Jove
Visualize
Contact Us

Related Concept Videos

Protein and Protein Structure02:15

Protein and Protein Structure

87.6K
Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...
87.6K
Structural Protein Function01:56

Structural Protein Function

30.0K
Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity.  In bones and teeth, it mineralizes to...
30.0K
Structural Protein Function01:56

Structural Protein Function

3.3K
3.3K
Protein and Protein Structures02:15

Protein and Protein Structures

19.1K
19.1K
Additional Subnuclear Structures02:10

Additional Subnuclear Structures

5.4K
The eukaryotic nucleus is a double membrane-bound organelle that contains nearly all of the cell’s genetic material in the form of chromosomes. It is rightly called the “brain” of the cell as it shoulders the responsibility of responding to various physiological processes, stress, altered metabolic conditions, and other cellular signals. 
The nucleus contains many membrane-less subnuclear organelles or nuclear bodies, such as nucleoli, Cajal bodies, speckles,...
5.4K
Collagens are the Major Structural Proteins of ECM01:13

Collagens are the Major Structural Proteins of ECM

5.8K
Three main types of fibers are secreted by fibroblasts: collagen fibers, elastic fibers, and reticular fibers. Collagen fiber is made from fibrous protein subunits linked together to form a long, straight fiber. Collagen fibers, while flexible, have great tensile strength, resist stretching, and give ligaments and tendons their characteristic resilience and strength. These fibers hold connective tissues together, even during the body's movement.
Connective tissue proper includes loose...
5.8K

You might also read

Related Articles

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

Sort by
Same author

The Evolution of Lipids from Solvents to Substrates.

Annual review of biophysics·2025
Same author

Pannexins in the vasculature.

American journal of physiology. Heart and circulatory physiology·2025
Same author

Pannexin channels in the kidney.

American journal of physiology. Renal physiology·2025
Same author

Publisher Correction: Tetraspanin-enriched membrane domains regulate vascular leakage by altering membrane cholesterol accessibility to balance antagonistic GTPases.

Nature cardiovascular research·2025
Same author

Tetraspanin-enriched membrane domains regulate vascular leakage by altering membrane cholesterol accessibility to balance antagonistic GTPases.

Nature cardiovascular research·2025
Same author

Influenza viral infection at the plasma membrane is restricted by lipid composition.

Journal of virology·2025
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 Experiment Video

Updated: Feb 3, 2026

Incorporating Target Protein Structure Flexibility and Dynamics in Computational Drug Discovery Using Ensemble-Based Docking Analysis
08:49

Incorporating Target Protein Structure Flexibility and Dynamics in Computational Drug Discovery Using Ensemble-Based Docking Analysis

Published on: June 20, 2025

1.2K

Refinement of Highly Flexible Protein Structures using Simulation-Guided Spectroscopy.

Jennifer M Hays1, Marissa K Kieber2, Jason Z Li2

  • 1Departments of Biomedical Engineering and Molecular Physiology, University of Virginia, Box 800886, Charlottesvile, VA, 22908, USA.

Angewandte Chemie (International Ed. in English)
|November 6, 2018
PubMed
Summary

Determining the structures of flexible proteins is challenging. A new method uses molecular simulations and information theory to select experiments that best refine protein conformational ensembles, improving function understanding.

Keywords:
EPR spectroscopyconformational ensemblesmolecular dynamicsmutual informationprotein structures

More Related Videos

Deciphering the Structural Effects of Activating EGFR Somatic Mutations with Molecular Dynamics Simulation
15:05

Deciphering the Structural Effects of Activating EGFR Somatic Mutations with Molecular Dynamics Simulation

Published on: May 20, 2020

9.3K
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

2.8K

Related Experiment Videos

Last Updated: Feb 3, 2026

Incorporating Target Protein Structure Flexibility and Dynamics in Computational Drug Discovery Using Ensemble-Based Docking Analysis
08:49

Incorporating Target Protein Structure Flexibility and Dynamics in Computational Drug Discovery Using Ensemble-Based Docking Analysis

Published on: June 20, 2025

1.2K
Deciphering the Structural Effects of Activating EGFR Somatic Mutations with Molecular Dynamics Simulation
15:05

Deciphering the Structural Effects of Activating EGFR Somatic Mutations with Molecular Dynamics Simulation

Published on: May 20, 2020

9.3K
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

2.8K

Area of Science:

  • Biochemistry and Structural Biology
  • Computational Biology
  • Biophysics

Background:

  • Flexible proteins possess multiple structures, crucial for function but difficult to determine.
  • Spectroscopic data for these proteins are often sparse, limiting conformational refinement.
  • Experiment selection is a bottleneck in characterizing protein conformational ensembles.

Purpose of the Study:

  • To develop and validate an approach for selecting experiments that refine protein conformational ensembles.
  • To improve the understanding of protein function through accurate structural determination of flexible proteins.

Main Methods:

  • Utilized molecular simulations and information theory to guide experiment selection.
  • Applied the approach to three distinct flexible protein systems.
  • Systematically identified experiments to test mechanistic hypotheses or outperform structure-guided methods.

Main Results:

  • Successfully identified informative experiments for conformational refinement across diverse flexible proteins.
  • Demonstrated superior performance compared to structure-guided approaches in certain cases.
  • Validated the utility of the simulation- and information-theory based method.

Conclusions:

  • The developed approach effectively refines challenging, underdetermined protein conformational ensembles.
  • This method enhances the study of protein dynamics and function.
  • Provides a powerful tool for structural biologists studying flexible proteins.