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Related Concept Videos

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 Folding01:22

Protein Folding

Overview
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...
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...

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4D Imaging of Protein Aggregation in Live Cells
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4D Imaging of Protein Aggregation in Live Cells

Published on: April 5, 2013

Intramolecular Interactions between Folded and Disordered Regions Shape Ubiquilin Structure and Function.

Jessica K Niblo1, Nirbhik Acharya1, Maxwell B Watkins2

  • 1Department of Chemistry, Syracuse University, Syracuse, New York, USA.

Advanced Science (Weinheim, Baden-Wurttemberg, Germany)
|June 2, 2026
PubMed
Summary
This summary is machine-generated.

Multidomain proteins like ubiquilins (UBQLNs) can adopt different structures. Intramolecular interactions involving disordered regions influence their shape, suggesting varied functions across species.

Keywords:
IDR:folded domain interactionsNMRSAXSUbiquilincoarse grain modelsintramolecular interactionsintrinsically disordered proteinsmolecular dynamics simulationsmultidomain proteins

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Last Updated: Jun 3, 2026

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NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins
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Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biology

Background:

  • Multidomain proteins feature folded domains linked by intrinsically disordered regions.
  • These disordered regions provide flexibility, enabling unique protein structures and functions.
  • Understanding intramolecular interactions in multidomain proteins is crucial but remains limited.

Purpose of the Study:

  • To investigate intramolecular interactions between folded domains and disordered regions in ubiquilins (UBQLNs).
  • To determine how these interactions affect multidomain protein structure and function.
  • To explore functional diversity among UBQLN homologs.

Main Methods:

  • Biophysical techniques
  • Computational simulations
  • Comparative analysis of eukaryotic UBQLN homologs

Main Results:

  • Interactions between folded domains in yeast UBQLN (Dsk2) favor a closed topology.
  • Disordered regions and the central STI1 domain modulate this closed topology.
  • Disordered:folded domain interactions vary across different eukaryotic UBQLN homologs.

Conclusions:

  • Intramolecular interactions significantly influence multidomain protein architecture.
  • Variations in these interactions suggest functional divergence among UBQLN proteins.
  • The study highlights potential differences in protein quality control mechanisms across eukaryotes.