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Related Concept Videos

Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

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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...
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The gastrointestinal tract is susceptible to various disorders. If the lower esophageal sphincter is damaged, stomach acid can flow back into the esophagus, causing irritation and inflammation of the lining. This condition is called gastroesophageal reflux disease (known as heartburn) and may cause chest pain and difficulty swallowing. In the stomach, prolonged use of nonsteroidal anti-inflammatory drugs like aspirin, chronic alcohol consumption, bacterial infections such as Helicobacter...
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Disorders of erythrocytes, or red blood cells (RBCs), include a range of conditions affecting their number, shape, or function.
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Mapping the Structure-Function Relationships of Disordered Oncogenic Transcription Factors Using Transcriptomic Analysis
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Intrinsically disordered domains: Sequence ➔ disorder ➔ function relationships.

Jianhong Zhou1,2, Christopher J Oldfield3, Wenying Yan2

  • 1Center for Computational Biology and Bioinformatics, Indiana University School of Medicine, Indianapolis, Indiana.

Protein Science : a Publication of the Protein Society
|July 13, 2019
PubMed
Summary
This summary is machine-generated.

Conserved protein sequences can surprisingly vary in disorder and structure content. This finding expands our understanding of how protein sequence, disorder, and function are interconnected.

Keywords:
disorder-function relationshipsdisorder-to-structure transitionsintrinsically disordered domains

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Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins
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Area of Science:

  • Biochemistry
  • Bioinformatics
  • Structural Biology

Background:

  • Disordered domains are crucial for protein interactions but lack systematic characterization.
  • They differ from interactions involving structured domains or molecular recognition features (MoRFs).

Purpose of the Study:

  • To investigate sequence-disorder-function relationships in probable disordered domains (PDDs).
  • To analyze PDDs identified from the Pfam database.

Main Methods:

  • Collected Pfam seed proteins containing at least one PDD sequence.
  • Analyzed sequence-disorder-function relationships using bioinformatics approaches.

Main Results:

  • Conserved sequences within domains can exhibit significant variations in predicted disorder and structure.
  • Homologues of a single domain can evolve between structured and disordered states.

Conclusions:

  • Protein sequence conservation does not always equate to conserved disorder or structure.
  • This enriches the paradigm of sequence-disorder ensemble-function relationships.