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Sensitivity to chirality correlates in a continuum with protein disorder
Lucía Álvarez1, Lucía Beatriz Chemes2
1Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Université Paris-Saclay, Gif-sur-Yvette, France.
Trends in Biochemical Sciences
|May 2, 2025
Summary
Intrinsically disordered proteins (IDPs) exhibit a spectrum of chiral sensitivity. Highly ordered protein complexes are strongly affected by chirality, while increasingly disordered proteins show reduced sensitivity.
Area of Science:
- Biochemistry
- Structural Biology
- Protein Science
Background:
- Intrinsically disordered proteins (IDPs) challenge traditional structure-function paradigms due to their dynamic nature.
- Understanding the biophysical properties of IDPs is crucial for deciphering their biological roles.
Purpose of the Study:
- To investigate the relationship between protein disorder and sensitivity to chirality.
- To explore how conformational flexibility influences chiral recognition in protein complexes.
Main Methods:
- Utilized biophysical techniques to assess chiral sensitivity across a range of protein structures.
- Analyzed protein complexes with varying degrees of intrinsic disorder.
Main Results:
- A continuum of chiral sensitivity was observed, correlating with the degree of protein disorder.
- Folded protein complexes demonstrated high sensitivity to chirality.
- Progressively disordered protein complexes exhibited significantly decreased sensitivity to chirality.
Conclusions:
- Protein disorder modulates chiral recognition, offering a new perspective on the protein structure-function paradigm.
- The findings suggest that conformational flexibility in IDPs can reduce constraints imposed by chirality.
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