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Related Concept Videos

Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

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...
Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

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...
Protein Folding01:22

Protein Folding

Overview
Protein Folding01:25

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Folding01:22

Protein Folding

Overview
Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

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 form...

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NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins
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Characterization of disordered proteins with ENSEMBLE.

Mickaël Krzeminski1, Joseph A Marsh, Chris Neale

  • 1Molecular Structure & Function Program, Hospital for Sick Children, Toronto, ON M5G 1X8, Canada.

Bioinformatics (Oxford, England)
|December 13, 2012
PubMed
Summary

ENSEMBLE is a new computational tool that models disordered protein structures using experimental data. This latest version offers an improved user interface and advanced data analysis for better insights into protein conformations.

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Related Experiment Videos

Last Updated: May 16, 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

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

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

Area of Science:

  • Computational biology
  • Structural biology
  • Biophysics

Background:

  • Disordered proteins lack a stable three-dimensional structure.
  • Understanding their conformational ensemble is crucial for biological function.
  • Existing methods may not fully capture the dynamic nature of these proteins.

Purpose of the Study:

  • To introduce the latest version of the ENSEMBLE program.
  • To provide an enhanced computational approach for modeling disordered protein structures.
  • To improve accessibility and usability for researchers.

Main Methods:

  • ENSEMBLE utilizes experimental data to determine a set of protein conformations.
  • The program represents the structural ensemble of unfolded or intrinsically disordered proteins.
  • The latest version features an intuitive user interface and new data treatment/analysis methods.

Main Results:

  • The enhanced ENSEMBLE program facilitates general release.
  • New approaches for data treatment and result analysis are incorporated.
  • The tool provides a comprehensive representation of protein structural ensembles.

Conclusions:

  • The updated ENSEMBLE program offers a powerful and accessible tool for studying disordered proteins.
  • It enables a more accurate representation of protein structural ensembles.
  • This advancement aids in understanding the function of intrinsically disordered proteins.