Taurine Induces an Ordered but Functionally Inactive Conformation in Intrinsically Disordered Casein Proteins
Mohd Younus Bhat1, Laishram Rajendrakumar Singh2, Tanveer Ali Dar3
1Department of Clinical Biochemistry, University of Kashmir, Srinagar, J&K, 190006, India.
Scientific Reports
|February 28, 2020
Summary
Osmolytes can either stabilize or destabilize intrinsically disordered proteins (IDPs). Specific osmolytes like taurine and TMAO induce structural collapse in IDPs, impacting their function and potentially contributing to disease.
Area of Science:
- Biochemistry
- Molecular Biology
- Proteomics
Background:
- Intrinsically disordered proteins (IDPs) are crucial for cellular processes like signaling and transcription.
- Maintaining the disordered state is essential for IDP function.
- Osmolytes are known to modulate macromolecular structure and stability.
Purpose of the Study:
- To investigate the impact of various osmolytes on the structure and function of two model IDPs: α- and β-casein.
- To determine if osmolytes act as folding inducers or folding evaders for IDPs.
Main Methods:
- Treatment of α- and β-casein with different classes of osmolytes.
- Analysis of structural and functional integrity changes in IDPs.
Main Results:
- Osmolytes were classified as either folding inducers or folding evaders.
- Folding evaders showed no significant effect on IDP structure or function.
- Taurine and TMAO acted as folding inducers, causing structural collapse and altering IDP integrity.
Conclusions:
- Osmolytes differentially regulate intrinsically disordered proteins.
- Osmolyte-induced changes in IDPs may play a role in disease pathologies.
- This study provides insights into the osmolyte-IDP interaction
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