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The function of proteins depends on their native three-dimensional structure, which is dictated by the amino acid sequence of the specific protein. Folding of the polypeptide chain takes place under specific conditions that energetically favor the folded conformation. In contrast, protein denaturation occurs spontaneously under unfavorable conditions that disrupt the integrity of the folded conformation. Thus, the chemical and physical environment of a protein, such as significant changes in pH...
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Updated: Aug 23, 2025

Analysis of AtHIRD11 Intrinsic Disorder and Binding Towards Metal Ions by Capillary Gel Electrophoresis and Affinity Capillary Electrophoresis
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Intrinsic protein disorder uncouples affinity from binding specificity.

Tamas Lazar1,2, Agnes Tantos3, Peter Tompa1,2,3

  • 1VIB-VUB Center for Structural Biology, Flanders Institute for Biotechnology (VIB), Brussels, Belgium.

Protein Science : a Publication of the Protein Society
|October 28, 2022
PubMed
Summary
This summary is machine-generated.

Intrinsically disordered proteins (IDPs) exhibit unique binding properties. Our study reveals that protein disorder decouples binding specificity from strength, challenging previous assumptions in the field.

Keywords:
IDPsbinding strengthconservationdisordered protein complexesspecificitystructural disorder

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

  • Biochemistry
  • Structural Biology
  • Molecular Biology

Background:

  • Intrinsically disordered proteins (IDPs) and their regions (IDRs) often bind targets through induced folding.
  • Prevailing theories suggest IDPs "uncouple" specificity from binding strength due to entropic penalties.
  • These assumptions are based on limited evidence and vague definitions of specificity.

Purpose of the Study:

  • To investigate the relationship between binding affinity and specificity in intrinsically disordered protein complexes.
  • To analyze a dataset of well-characterized IDP/globular and globular/globular protein complexes.
  • To provide evidence-based insights into the functional advantages of intrinsically disordered proteins.

Main Methods:

  • Creation and analysis of a comprehensive dataset of IDP/globular and globular/globular protein complexes.
  • Inclusion of complexes with known atomic structures and interaction free energies (ΔG, Kd).
  • Comparative analysis of affinity distributions between IDP and globular protein complexes.

Main Results:

  • Affinity distributions differ significantly between IDP/globular and globular/globular complexes.
  • Specificity in IDPs/IDRs is not necessarily correlated with weaker binding strength.
  • Protein disorder expands the range of weak interactions, potentially impacting biological regulation.

Conclusions:

  • The study challenges the long-held notion that IDPs inherently trade specificity for weaker binding.
  • Structural disorder in proteins can uncouple the strict correlation between binding specificity and strength.
  • The expanded spectrum of weak interactions mediated by IDPs may have significant regulatory roles.