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

Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

19.4K
Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
19.4K
Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

2.8K
2.8K
Protein and Protein Structure02:15

Protein and Protein Structure

87.5K
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...
87.5K
Structural Protein Function01:56

Structural Protein Function

29.9K
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...
29.9K
Structural Protein Function01:56

Structural Protein Function

3.3K
3.3K
Protein and Protein Structures02:15

Protein and Protein Structures

19.1K
19.1K

You might also read

Related Articles

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

Sort by
Same author

Alternative Splicing of a Structured Partner Alters the Folding-Upon-Binding Trajectory of an Intrinsically Disordered Protein.

Journal of the American Chemical Society·2026
Same author

DL3D: visual representation of conformational ensembles of domain-linker-domain proteins.

BMC bioinformatics·2026
Same author

LinkCraft: An interactive tool for the design of flexible linkers.

Journal of molecular biology·2026
Same author

Membrane cholesterol modulates engagement of β-arrestin with the ghrelin receptor.

Communications biology·2026
Same author

Toward a unified framework for determining conformational ensembles of disordered proteins.

Nature methods·2026
Same author

Radiation-response in <i>Deinococcus</i> bacteria: characterization of the transient IrrE-DdrO heterodimer complex.

FEMS microbes·2026

Related Experiment Video

Updated: Feb 1, 2026

Author Spotlight: Unlocking the World of Intrinsically Disordered Regions with Cellular Sensing and Responses
05:13

Author Spotlight: Unlocking the World of Intrinsically Disordered Regions with Cellular Sensing and Responses

Published on: January 12, 2024

1.5K

Realistic Ensemble Models of Intrinsically Disordered Proteins Using a Structure-Encoding Coil Database.

Alejandro Estaña1, Nathalie Sibille2, Elise Delaforge2

  • 1L-CNRS, Université de Toulouse, CNRS, Toulouse, France; Centre de Biochimie Structurale. INSERM, CNRS, Université de Montpellier, Montpellier, France.

Structure (London, England : 1993)
|December 18, 2018
PubMed
Summary
This summary is machine-generated.

Intrinsically disordered proteins (IDPs) are crucial for cell function. This study develops a new method combining sequence-independent and dependent strategies to accurately model IDP structures, aiding in protein design.

Keywords:
conformational ensembleconformational samplingintrinsically disordered proteinsprotein fragment databaseresidual dipolar couplings

More Related Videos

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins
07:24

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins

Published on: September 23, 2021

2.3K
Combining Wet and Dry Lab Techniques to Guide the Crystallization of Large Coiled-coil Containing Proteins
11:14

Combining Wet and Dry Lab Techniques to Guide the Crystallization of Large Coiled-coil Containing Proteins

Published on: January 6, 2017

8.4K

Related Experiment Videos

Last Updated: Feb 1, 2026

Author Spotlight: Unlocking the World of Intrinsically Disordered Regions with Cellular Sensing and Responses
05:13

Author Spotlight: Unlocking the World of Intrinsically Disordered Regions with Cellular Sensing and Responses

Published on: January 12, 2024

1.5K
Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins
07:24

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins

Published on: September 23, 2021

2.3K
Combining Wet and Dry Lab Techniques to Guide the Crystallization of Large Coiled-coil Containing Proteins
11:14

Combining Wet and Dry Lab Techniques to Guide the Crystallization of Large Coiled-coil Containing Proteins

Published on: January 6, 2017

8.4K

Area of Science:

  • Biochemistry and Structural Biology
  • Computational Biology
  • Molecular Biophysics

Background:

  • Intrinsically disordered proteins (IDPs) are vital for cellular processes like signaling and regulation.
  • Characterizing the structures of IDPs and their interaction regions is a significant challenge in structural biology.
  • Existing methods often struggle to accurately represent the dynamic and flexible nature of IDPs.

Purpose of the Study:

  • To develop a novel computational approach for predicting the structures of intrinsically disordered proteins.
  • To integrate experimental data with sequence-based and sequence-independent structural information.
  • To improve the accuracy of ensemble modeling for both fully and partially disordered protein regions.

Main Methods:

  • Exploiting structural information from tripeptide fragments in coil regions of known protein structures.
  • Developing a building strategy that disregards sequence context for fully disordered regions.
  • Incorporating sequence-dependent structural preferences for modeling partially structured motifs.
  • Utilizing experimental data, including nuclear magnetic resonance residual dipolar couplings and small-angle X-ray scattering.

Main Results:

  • A simple building approach using tripeptide fragments effectively represents fully disordered protein regions.
  • Considering sequence context is essential for accurately describing partially structured motifs within IDPs.
  • Combining both strategies generates ensemble models that accurately capture secondary structural classes and populations of partially structured regions.
  • Validated models against experimental data for multiple IDPs.

Conclusions:

  • A hybrid modeling strategy effectively characterizes the structural ensembles of intrinsically disordered proteins.
  • This approach enhances the ability to predict structures and design novel disordered proteins.
  • The findings open new avenues for studying the functional roles of IDPs.