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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
Protein Organization01:24

Protein Organization

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.

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Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web
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Published on: July 16, 2017

Relating protein conformational changes to packing efficiency and disorder.

Nitin Bhardwaj1, Mark Gerstein

  • 1Program in Computational Biology and Bioinformatics, Yale University, New Haven, CT 06520, USA.

Protein Science : a Publication of the Protein Society
|May 28, 2009
PubMed
Summary
This summary is machine-generated.

Protein conformational changes impact packing efficiency and disorder, especially at dynamic interfaces. Core regions remain stable, while interfaces exhibit elasticity, offering insights into protein dynamics.

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Last Updated: Jun 22, 2026

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web
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Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins
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Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins

Published on: September 23, 2021

Area of Science:

  • Biochemistry
  • Structural Biology
  • Computational Biology

Background:

  • Protein conformational changes are vital for biochemical processes.
  • Factors driving protein motion are known, but structural impacts are less understood.
  • Protein packing efficiency is critical for stability and function.

Purpose of the Study:

  • To investigate the relationship between protein conformational changes and structural metrics like packing efficiency and disorder.
  • To analyze how packing efficiency and disorder change dynamically during protein conformational shifts.
  • To identify regions within proteins that exhibit the most significant structural changes during conformational transitions.

Main Methods:

  • Analysis of protein conformational changes in relation to packing efficiency and disorder.
  • Studying proteins with alternate conformations to correlate motion with packing efficiency changes.
  • Examining packing efficiency changes within secondary structure contexts (helices, bends).
  • Relating protein disorder to atomic displacement and packing efficiency changes.

Main Results:

  • Residues with altered packing efficiency exhibit greater motion.
  • Significant packing changes occur at dynamic interfaces formed during conformational shifts.
  • Helix residues show minimal packing change, while bend residues show the most.
  • Marginally disordered residues display higher dislocation and packing changes, often at interfaces.
  • Protein cores remain largely unchanged, while interfaces show increased elasticity.

Conclusions:

  • Protein conformational changes are intrinsically linked to dynamic alterations in packing efficiency and disorder.
  • Dynamic interfaces are key sites of structural flexibility during protein motion.
  • Understanding these dynamic structural changes provides insights into protein function and regulation.