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Related Concept Videos

Intrinsically Disordered Proteins02:18

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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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Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
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Updated: Sep 15, 2025

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins
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Design of intrinsically disordered region binding proteins.

Kejia Wu1,2,3, Hanlun Jiang1,2,4, Derrick R Hicks1,2

  • 1Department of Biochemistry, University of Washington, Seattle, WA, USA.

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Summary

Scientists developed a new method to design proteins that bind to intrinsically disordered proteins (IDPs). This breakthrough enables targeting challenging biological molecules, offering potential for new diagnostics and therapeutics.

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Area of Science:

  • Proteomics
  • Structural Biology
  • Protein Design

Background:

  • Intrinsically disordered proteins (IDPs) are crucial in biological processes but difficult to target due to their lack of fixed structures.
  • The high variability in IDP sequence and conformation presents a significant challenge for drug discovery and molecular recognition.

Purpose of the Study:

  • To develop a generalizable computational approach for designing proteins that can bind to intrinsically disordered protein regions.
  • To create specific and high-affinity binders for a diverse set of unstructured protein targets.

Main Methods:

  • A novel design strategy was employed to create proteins with binding pockets complementary to extended conformations of IDPs.
  • Computational design was followed by experimental validation, including affinity measurements and in-cell functionality tests.

Main Results:

  • Successfully designed binders for 39 diverse intrinsically disordered targets, achieving high affinities (100 pM to 100 nM) in 34 instances.
  • Designed binders demonstrated functionality within cellular environments and as specific detection reagents.
  • All-by-all binding assays confirmed the high specificity of the designed binders for their intended targets.

Conclusions:

  • The developed protein design approach represents a significant advancement in addressing the challenge of intrinsically disordered protein recognition.
  • This method offers a powerful tool for targeting IDPs, paving the way for new applications in molecular biology and medicine.